From 194d4f09fcb5218d9e158db64b82961c00416051 Mon Sep 17 00:00:00 2001 From: Martina Summer-Kutmon Date: Tue, 5 May 2015 22:50:04 +0200 Subject: [PATCH] added junit test --- .classpath | 4 +- lib/jdom-2.0.6.jar | Bin 0 -> 304924 bytes lib/jdom.jar | Bin 152797 -> 0 bytes resources/drugbank-example.xml | 3202 +++++++++++++++++++++++++ src/msk/drugbank4/DrugBankParser.java | 10 +- test/msk/drugbank4/test/Test.java | 42 + 6 files changed, 3252 insertions(+), 6 deletions(-) create mode 100644 lib/jdom-2.0.6.jar delete mode 100644 lib/jdom.jar create mode 100644 resources/drugbank-example.xml create mode 100644 test/msk/drugbank4/test/Test.java diff --git a/.classpath b/.classpath index 83eed7d..ffcf8c5 100644 --- a/.classpath +++ b/.classpath @@ -1,7 +1,9 @@ - + + + diff --git a/lib/jdom-2.0.6.jar b/lib/jdom-2.0.6.jar new file mode 100644 index 0000000000000000000000000000000000000000..2850ca10cf9c97e9aed8cf35751d1448030a84c3 GIT binary patch literal 304924 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zz>}}-33d|(?c29t2$+rt0Fqx8_QF*V6n}wT)H*0wQx2l+SJFl6 zBx$90d;j`Ev8cfHWkSGprU2!xKONO~zv3?QUU_>RJ+s>ttYeU3zyZ9lMfj%w)KvXS z1mff`{&VxR+yBa(;e|2sEAQ&ztGAwgd$anvd7A4_eC+6-@wXTM=B|l9d2Z)dct3|P zFCNjK_E5a3@XbxLe%@db0{mw?ed`Tw-9qc;4Q}oV^z#N<(0{qX?IyXo`NL0O8{%() zf7lA*rouO0iT}w*Mg1H9!un!2Uy#3fgPX4l|Ga?;FdTlF8eKQ})t85F0&l*0_7kXq zdn@n{FQVOK-+XK7C)*wWuk7Dd;x`w<|AcyyUV+|RlzVeo{7qeNuI~Mb1qX&2E)9DV zd%K(6TvPQEHbVCc>^Cc{ZYp?lsmo7h+{4?M|LFz+WN*OwF5s&i7?40^2dZqa{{v|f BBZ2?` diff --git a/resources/drugbank-example.xml b/resources/drugbank-example.xml new file mode 100644 index 0000000..4d87693 --- /dev/null +++ b/resources/drugbank-example.xml @@ -0,0 +1,3202 @@ + + + + DB00001 + BIOD00024 + BTD00024 + Lepirudin + Lepirudin is identical to natural hirudin except for substitution of leucine for isoleucine at the N-terminal end of the molecule and the absence of a sulfate group on the tyrosine at position 63. It is produced via yeast cells. Bayer ceased the production of lepirudin (Refludan) effective May 31, 2012. + 120993-53-5 + + approved + + # Smythe MA, Stephens JL, Koerber JM, Mattson JC: A comparison of lepirudin and argatroban outcomes. Clin Appl Thromb Hemost. 2005 Oct;11(4):371-4. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16244762 +# Tardy B, Lecompte T, Boelhen F, Tardy-Poncet B, Elalamy I, Morange P, Gruel Y, Wolf M, Francois D, Racadot E, Camarasa P, Blouch MT, Nguyen F, Doubine S, Dutrillaux F, Alhenc-Gelas M, Martin-Toutain I, Bauters A, Ffrench P, de Maistre E, Grunebaum L, Mouton C, Huisse MG, Gouault-Heilmann M, Lucke V: Predictive factors for thrombosis and major bleeding in an observational study in 181 patients with heparin-induced thrombocytopenia treated with lepirudin. Blood. 2006 Sep 1;108(5):1492-6. Epub 2006 May 11. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16690967 +# Lubenow N, Eichler P, Lietz T, Greinacher A: Lepirudin in patients with heparin-induced thrombocytopenia - results of the third prospective study (HAT-3) and a combined analysis of HAT-1, HAT-2, and HAT-3. J Thromb Haemost. 2005 Nov;3(11):2428-36. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16241940 +# Askari AT, Lincoff AM: Antithrombotic Drug Therapy in Cardiovascular Disease. 2009 Oct; pp. 440–. ISBN 9781603272346. "Google books":http://books.google.com/books?id=iadLoXoQkWEC&pg=PA440. + + For the treatment of heparin-induced thrombocytopenia + Lepirudin is used to break up clots and to reduce thrombocytopenia. It binds to thrombin and prevents thrombus or clot formation. It is a highly potent, selective, and essentially irreversible inhibitor of thrombin and clot-bond thrombin. Lepirudin requires no cofactor for its anticoagulant action. Lepirudin is a recombinant form of hirudin, an endogenous anticoagulant found in medicinal leeches. + Lepirudin forms a stable non-covalent complex with alpha-thrombin, thereby abolishing its ability to cleave fibrinogen and initiate the clotting cascade. The inhibition of thrombin prevents the blood clotting cascade. + In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased. + Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. However, con-clusive data are not available. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) and other fragments of the parent drug. + Bioavailability is 100% following injection. + Approximately 1.3 hours + + Lepirudin is thought to be metabolized by release of amino acids via catabolic hydrolysis of the parent drug. About 48% of the administration dose is excreted in the urine which consists of unchanged drug (35%) and other fragments of the parent drug. + * 12.2 L [Healthy young subjects (n = 18, age 18-60 years)] +* 18.7 L [Healthy elderly subjects (n = 10, age 65-80 years)] +* 18 L [Renally impaired patients (n = 16, creatinine clearance below 80 mL/min)] +* 32.1 L [HIT patients (n = 73)] + * 164 ml/min [Healthy 18-60 yrs] +* 139 ml/min [Healthy 65-80 yrs] +* 61 ml/min [renal impaired] +* 114 ml/min [HIT (Heparin-induced thrombocytopenia)] + + + Peptides + Organic Compounds + Organic Acids + Carboxylic Acids and Derivatives + Amino Acids, Peptides, and Analogues + + + + Hirudin variant-1 + + + + Refludan + + + + + Bayer Healthcare + http://www.bayerhealthcare.com + + + Berlex Labs + http://www.berlex.com + + + + Bayer healthcare pharmaceuticals inc + + + + Refludan 50 mg vial + 273.19 + vial + + + + + Antithrombins + + + + Fibrinolytic Agents + + + + + Humans and other mammals + + + + + BLOOD AND BLOOD FORMING ORGANS + ANTITHROMBOTIC AGENTS + ANTITHROMBOTIC AGENTS + Direct thrombin inhibitors + + + + 20:12.04.12 + + + + 1339104 + Canada + 1997-07-29 + 2014-07-29 + + + 5180668 + United States + 1993-01-19 + 2010-01-19 + + + + + + DB01381 + Ginkgo biloba + Additive anticoagulant/antiplatelet effects may increase bleed risk. Concomitant therapy should be avoided. + + + DB00374 + Treprostinil + The prostacyclin analogue, Treprostinil, increases the risk of bleeding when combined with the anticoagulant, Lepirudin. Monitor for increased bleeding during concomitant thearpy. + + + + >DB00001 sequence +LVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIP +EEYLQ + + + + Melting Point + 65 °C + Otto, A. & Seckler, R. Eur. J. Biochem. 202:67-73 (1991) + + + Hydrophobicity + -0.777 + + + + Isoelectric Point + 4.04 + + + + Molecular Weight + 6963.4250 + + + + Molecular Formula + C287H440N80O110S6 + + + + + + KEGG Drug + D06880 + + + National Drug Code Directory + 50419-150-57 + + + PharmGKB + PA450195 + + + UniProtKB + P01050 + + + Wikipedia + Lepirudin + + + + + RxList + http://www.rxlist.com/cgi/generic/lepirudin.htm + + + Drugs.com + http://www.drugs.com/cdi/lepirudin.html + + + + + SMP00278 + Lepirudin Action Pathway + + + DB00001 + Lepirudin + + + DB01373 + Calcium + + + + P00734 + P00748 + P02452 + P03952 + P03951 + P00740 + P00451 + P12259 + P00742 + P02671 + P02675 + P02679 + P00488 + P05160 + P00747 + P00750 + P08709 + P13726 + Q9BQB6 + P38435 + + + + + + + + + BE0000048 + Prothrombin + Human + + inhibitor + + # Turpie AG: Anticoagulants in acute coronary syndromes. Am J Cardiol. 1999 Sep 2;84(5A):2M-6M. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10505536 +# Warkentin TE: Venous thromboembolism in heparin-induced thrombocytopenia. Curr Opin Pulm Med. 2000 Jul;6(4):343-51. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10912644 +# Eriksson BI: New therapeutic options in deep vein thrombosis prophylaxis. Semin Hematol. 2000 Jul;37(3 Suppl 5):7-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11055889 +# Fabrizio MC: Use of ecarin clotting time (ECT) with lepirudin therapy in heparin-induced thrombocytopenia and cardiopulmonary bypass. J Extra Corpor Technol. 2001 May;33(2):117-25. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11467439 +# Szaba FM, Smiley ST: Roles for thrombin and fibrin(ogen) in cytokine/chemokine production and macrophage adhesion in vivo. Blood. 2002 Feb 1;99(3):1053-9. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11807012 +# Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11752352 + yes + + Prothrombin + Involved in blood clotting cascade + Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C + F2 + 11p11-q12 + Secreted protein; extracellular space + None + + 5.7 + 70037.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3535 + + + GenAtlas + F2 + + + GeneCards + F2 + + + GenBank Gene Database + M17262 + + + GenBank Protein Database + 339641 + + + UniProtKB + P00734 + + + UniProt Accession + THRB_HUMAN + + + + Activated Factor II [IIa] + Coagulation factor II + EC 3.4.21.5 + Prothrombin precursor + Thrombin + + >Prothrombin precursor +MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC +VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV +NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE +CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA +QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG +DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI +DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN +DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP +VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST +RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY +GFYTHVFRLKKWIQKVIDQFGE + >1869 bp +ATGGCGCACGTCCGAGGCTTGCAGCTGCCTGGCTGCCTGGCCCTGGCTGCCCTGTGTAGC +CTTGTGCACAGCCAGCATGTGTTCCTGGCTCCTCAGCAAGCACGGTCGCTGCTCCAGCGG +GTCCGGCGAGCCAACACCTTCTTGGAGGAGGTGCGCAAGGGCAACCTAGAGCGAGAGTGC +GTGGAGGAGACGTGCAGCTACGAGGAGGCCTTCGAGGCTCTGGAGTCCTCCACGGCTACG +GATGTGTTCTGGGCCAAGTACACAGCTTGTGAGACAGCGAGGACGCCTCGAGATAAGCTT +GCTGCATGTCTGGAAGGTAACTGTGCTGAGGGTCTGGGTACGAACTACCGAGGGCATGTG +AACATCACCCGGTCAGGCATTGAGTGCCAGCTATGGAGGAGTCGCTACCCACATAAGCCT +GAAATCAACTCCACTACCCATCCTGGGGCCGACCTACAGGAGAATTTCTGCCGCAACCCC +GACAGCAGCACCACGGGACCCTGGTGCTACACTACAGACCCCACCGTGAGGAGGCAGGAA +TGCAGCATCCCTGTCTGTGGCCAGGATCAAGTCACTGTAGCGATGACTCCACGCTCCGAA +GGCTCCAGTGTGAATCTGTCACCTCCATTGGAGCAGTGTGTCCCTGATCGGGGGCAGCAG +TACCAGGGGCGCCTGGCGGTGACCACACATGGGCTCCCCTGCCTGGCCTGGGCCAGCGCA +CAGGCCAAGGCCCTGAGCAAGCACCAGGACTTCAACTCAGCTGTGCAGCTGGTGGAGAAC +TTCTGCCGCAACCCAGACGGGGATGAGGAGGGCGTGTGGTGCTATGTGGCCGGGAAGCCT +GGCGACTTTGGGTACTGCGACCTCAACTATTGTGAGGAGGCCGTGGAGGAGGAGACAGGA +GATGGGCTGGATGAGGACTCAGACAGGGCCATCGAAGGGCGTACCGCCACCAGTGAGTAC +CAGACTTTCTTCAATCCGAGGACCTTTGGCTCGGGAGAGGCAGACTGTGGGCTGCGACCT +CTGTTCGAGAAGAAGTCGCTGGAGGACAAAACCGAAAGAGAGCTCCTGGAATCCTACATC +GACGGGCGCATTGTGGAGGGCTCGGATGCAGAGATCGGCATGTCACCTTGGCAGGTGATG +CTTTTCCGGAAGAGTCCCCAGGAGCTGCTGTGTGGGGCCAGCCTCATCAGTGACCGCTGG +GTCCTCACCGCCGCCCACTGCCTCCTGTACCCGCCCTGGGACAAGAACTTCACCGAGAAT +GACCTTCTGGTGCGCATTGGCAAGCACTCCCGCACAAGGTACGAGCGAAACATTGAAAAG +ATATCCATGTTGGAAAAGATCTACATCCACCCCAGGTACAACTGGCGGGAGAACCTGGAC +CGGGACATTGCCCTGATGAAGCTGAAGAAGCCTGTTGCCTTCAGTGACTACATTCACCCT +GTGTGTCTGCCCGACAGGGAGACGGCAGCCAGCTTGCTCCAGGCTGGATACAAGGGGCGG +GTGACAGGCTGGGGCAACCTGAAGGAGACGTGGACAGCCAACGTTGGTAAGGGGCAGCCC +AGTGTCCTGCAGGTGGTGAACCTGCCCATTGTGGAGCGGCCGGTCTGCAAGGACTCCACC +CGGATCCGCATCACTGACAACATGTTCTGTGCTGGTTACAAGCCTGATGAAGGGAAACGA +GGGGATGCCTGTGAAGGTGACAGTGGGGGACCCTTTGTCATGAAGAGCCCCTTTAACAAC +CGCTGGTATCAAATGGGCATCGTCTCATGGGGTGAAGGCTGTGACCGGGATGGGAAATAT +GGCTTCTACACACATGTGTTCCGCCTGAAGAAGTGGATACAGAAGGTCATTGATCAGTTT +GGAGAGTAG + + + PF00594 + Gla + + + PF00051 + Kringle + + + PF00089 + Trypsin + + + + + component + extracellular region + + + function + hydrolase activity + + + function + calcium ion binding + + + function + peptidase activity + + + function + ion binding + + + function + endopeptidase activity + + + function + cation binding + + + function + serine-type endopeptidase activity + + + function + binding + + + function + catalytic activity + + + function + thrombin activity + + + process + macromolecule metabolism + + + process + protein metabolism + + + process + proteolysis + + + process + cellular protein metabolism + + + process + organismal physiological process + + + process + regulation of body fluids + + + process + physiological process + + + process + hemostasis + + + process + blood coagulation + + + process + metabolism + + + + + + + + + + + DB00002 + BIOD00071 + BTD00071 + Cetuximab + Epidermal growth factor receptor binding FAB. Cetuximab is composed of the Fv (variable; antigen-binding) regions of the 225 murine EGFr monoclonal antibody specific for the N-terminal portion of human EGFr with human IgG1 heavy and kappa light chain constant (framework) regions. + 205923-56-4 + + approved + + + + For treatment of EGFR-expressing metastatic colorectal cancer in patients who are refractory to other irinotecan-based chemotherapy regimens. Cetuximab is also indicated for treatment of squamous cell carcinoma of the head and neck in conjucntion with radiation therapy. + Used in the treatment of colorectal cancer, cetuximab binds specifically to the epidermal growth factor receptor (EGFr, HER1, c-ErbB-1) on both normal and tumor cells. EGFr is over-expressed in many colorectal cancers. Cetuximab competitively inhibits the binding of epidermal growth factor (EGF) and other ligands, such as transforming growth factor–alpha. Binding of cetuximab to the EGFr blocks phosphorylation and activation of receptor-associated kinases, resulting in inhibition of cell growth, induction of apoptosis, decreased matrix metalloproteinase secretion and reduced vascular endothelial growth factor production. + Cetuximab binds to the epidermal growth factor receptor (EGFr) on both normal and tumor cells. EGFr is over-expressed in many colorectal cancers. Cetuximab competitively inhibits the binding of epidermal growth factor (EGF) and TGF alpha, thereby reducing their effects on cell growth and metastatic spread. + Single doses of cetuximab higher than 500 mg/m<sup>2</sup> have not been tested. There is no experience with overdosage in human clinical trials. + + + + + 114 hrs + + + + + + + Peptides + Organic Compounds + Organic Acids + Carboxylic Acids and Derivatives + Amino Acids, Peptides, and Analogues + + + + Anti EGFR + IMC-C225 + + + + Erbitux + 66733-948_63642894-aaa8-4e5b-97fd-3c44aeeedd8a + 66733-948 + 2004-02-12 + + solution + 2 mg/mL + intravenous + BLA125084 + false + false + true + US + FDA NDC + + + Erbitux + 66733-958_63642894-aaa8-4e5b-97fd-3c44aeeedd8a + 66733-958 + 2007-10-02 + + solution + 2 mg/mL + intravenous + BLA125084 + false + false + true + US + FDA NDC + + + Erbitux + + + + + solution + 2 mg + intravenous + + false + false + true + Canada + DPD + + + + + + + Cardinal Health + http://www.cardinal.com + + + Catalent Pharma Solutions + http://www.catalent.com + + + ImClone Systems Inc. + http://www.imclone.com + + + Oso Biopharmaceuticals Manufacturing LLC + + + + + + + + Antineoplastic Agents + + + + + Humans and other mammals + + + +

Solution + intravenous + 2 mg + + +
Solution
+ intravenous + 2 mg/mL +
+ + + + ANTINEOPLASTIC AND IMMUNOMODULATING AGENTS + ANTINEOPLASTIC AGENTS + OTHER ANTINEOPLASTIC AGENTS + Monoclonal antibodies + + + + + + 1340417 + Canada + 1999-03-02 + 2016-03-02 + + + + + + >Cetuximab heavy chain +QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYN +TPFTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAA +STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG +LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSPKSCDKTHTCPPCPAPELL +GGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQ +YNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR +DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS +RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK + >Cetuximab light chain +DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPS +RFSGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPP +SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT +LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGA + + + + Melting Point + 61 °C (FAB fragment), 71 °C (whole mAb) + Vermeer, A.W.P. & Norde, W., Biophys. J. 78:394-404 (2000) + + + Hydrophobicity + -0.413 + + + + Isoelectric Point + 8.48 + + + + Molecular Weight + 145781.6000 + + + + Molecular Formula + C6484H10042N1732O2023S36 + + + + + + National Drug Code Directory + 66733-948-23 + + + GenBank + J00228 + + + PharmGKB + PA10040 + + + Wikipedia + Cetuximab + + + + + RxList + http://www.rxlist.com/cgi/generic3/erbitux.htm + + + Drugs.com + http://www.drugs.com/cdi/cetuximab.html + + + + + SMP00474 + Cetuximab Action Pathway + + + DB00002 + Cetuximab + + + + P00533 + + + + + + + Low affinity immunoglobulin gamma Fc region receptor II-a + FCGR2A + P12318 + rs1801274 + + H allelle + Increased progression free survival + 17704420 + + + Low affinity immunoglobulin gamma Fc region receptor III-A + FCGR3A + P08637 + rs396991 + + A > C + Better response to drug therapy (longer progression free survival) with the F allele + 17704420 + + + + + + BE0000767 + Epidermal growth factor receptor + Human + + antagonist + + # Hosokawa N, Yamamoto S, Uehara Y, Hori M, Tsuchiya KS: Effect of thiazinotrienomycin B, an ansamycin antibiotic, on the function of epidermal growth factor receptor in human stomach tumor cells. J Antibiot (Tokyo). 1999 May;52(5):485-90. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10480573 +# Wakita H, Takigawa M: Activation of epidermal growth factor receptor promotes late terminal differentiation of cell-matrix interaction-disrupted keratinocytes. J Biol Chem. 1999 Dec 24;274(52):37285-91. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10601294 +# Suwa T, Ueda M, Jinno H, Ozawa S, Kitagawa Y, Ando N, Kitajima M: Epidermal growth factor receptor-dependent cytotoxic effect of anti-EGFR antibody-ribonuclease conjugate on human cancer cells. Anticancer Res. 1999 Sep-Oct;19(5B):4161-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10628369 +# Burke P, Schooler K, Wiley HS: Regulation of epidermal growth factor receptor signaling by endocytosis and intracellular trafficking. Mol Biol Cell. 2001 Jun;12(6):1897-910. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11408594 +# Viloria-Petit A, Crombet T, Jothy S, Hicklin D, Bohlen P, Schlaeppi JM, Rak J, Kerbel RS: Acquired resistance to the antitumor effect of epidermal growth factor receptor-blocking antibodies in vivo: a role for altered tumor angiogenesis. Cancer Res. 2001 Jul 1;61(13):5090-101. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11431346 +# Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11752352 + yes + + Epidermal growth factor receptor + Involved in transmembrane receptor protein tyrosine kinase activity + Isoform 2/truncated isoform may act as an antagonist + EGFR + 7p12 + Cell membrane; single-pass type I membrane protein. Isoform 2:Secreted protein + 646-668 + + 6.67 + 134279.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3236 + + + GenAtlas + EGFR + + + GeneCards + EGFR + + + GenBank Gene Database + X00588 + + + GenBank Protein Database + 757924 + + + UniProtKB + P00533 + + + UniProt Accession + EGFR_HUMAN + + + + EC 2.7.10.1 + Epidermal growth factor receptor precursor + Receptor tyrosine-protein kinase ErbB-1 + + >Epidermal growth factor receptor precursor +MRPSGTAGAALLALLAALCPASRALEEKKVCQGTSNKLTQLGTFEDHFLSLQRMFNNCEV +VLGNLEITYVQRNYDLSFLKTIQEVAGYVLIALNTVERIPLENLQIIRGNMYYENSYALA +VLSNYDANKTGLKELPMRNLQEILHGAVRFSNNPALCNVESIQWRDIVSSDFLSNMSMDF +QNHLGSCQKCDPSCPNGSCWGAGEENCQKLTKIICAQQCSGRCRGKSPSDCCHNQCAAGC +TGPRESDCLVCRKFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYV +VTDHGSCVRACGADSYEMEEDGVRKCKKCEGPCRKVCNGIGIGEFKDSLSINATNIKHFK +NCTSISGDLHILPVAFRGDSFTHTPPLDPQELDILKTVKEITGFLLIQAWPENRTDLHAF +ENLEIIRGRTKQHGQFSLAVVSLNITSLGLRSLKEISDGDVIISGNKNLCYANTINWKKL +FGTSGQKTKIISNRGENSCKATGQVCHALCSPEGCWGPEPRDCVSCRNVSRGRECVDKCN +LLEGEPREFVENSECIQCHPECLPQAMNITCTGRGPDNCIQCAHYIDGPHCVKTCPAGVM +GENNTLVWKYADAGHVCHLCHPNCTYGCTGPGLEGCPTNGPKIPSIATGMVGALLLLLVV +ALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQALLRILKETEFKKIKVLGS +GAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGI +CLTSTVQLITQLMPFGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAA +RNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSY +GVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPK +FRELIIEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMDEEDMDDVVDADEYLIPQ +QGFFSSPSTSRTPLLSSLSATSNNSTVACIDRNGLQSCPIKEDSFLQRYSSDPTGALTED +SIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLNPAPSRDPHYQDPHSTAVGNPEYLN +TVQPTCVNSTFDSPAHWAQKGSHQISLDNPDYQQDFFPKEAKPNGIFKGSTAENAEYLRV +APQSSEFIGA + >3633 bp +ATGCGACCCTCCGGGACGGCCGGGGCAGCGCTCCTGGCGCTGCTGGCTGCGCTCTGCCCG +GCGAGTCGGGCTCTGGAGGAAAAGAAAGTTTGCCAAGGCACGAGTAACAAGCTCACGCAG +TTGGGCACTTTTGAAGATCATTTTCTCAGCCTCCAGAGGATGTTCAATAACTGTGAGGTG +GTCCTTGGGAATTTGGAAATTACCTATGTGCAGAGGAATTATGATCTTTCCTTCTTAAAG +ACCATCCAGGAGGTGGCTGGTTATGTCCTCATTGCCCTCAACACAGTGGAGCGAATTCCT +TTGGAAAACCTGCAGATCATCAGAGGAAATATGTACTACGAAAATTCCTATGCCTTAGCA +GTCTTATCTAACTATGATGCAAATAAAACCGGACTGAAGGAGCTGCCCATGAGAAATTTA +CAGGAAATCCTGCATGGCGCCGTGCGGTTCAGCAACAACCCTGCCCTGTGCAACGTGGAG +AGCATCCAGTGGCGGGACATAGTCAGCAGTGACTTTCTCAGCAACATGTCGATGGACTTC +CAGAACCACCTGGGCAGCTGCCAAAAGTGTGATCCAAGCTGTCCCAATGGGAGCTGCTGG +GGTGCAGGAGAGGAGAACTGCCAGAAACTGACCAAAATCATCTGTGCCCAGCAGTGCTCC +GGGCGCTGCCGTGGCAAGTCCCCCAGTGACTGCTGCCACAACCAGTGTGCTGCAGGCTGC +ACAGGCCCCCGGGAGAGCGACTGCCTGGTCTGCCGCAAATTCCGAGACGAAGCCACGTGC +AAGGACACCTGCCCCCCACTCATGCTCTACAACCCCACCACGTACCAGATGGATGTGAAC +CCCGAGGGCAAATACAGCTTTGGTGCCACCTGCGTGAAGAAGTGTCCCCGTAATTATGTG +GTGACAGATCACGGCTCGTGCGTCCGAGCCTGTGGGGCCGACAGCTATGAGATGGAGGAA +GACGGCGTCCGCAAGTGTAAGAAGTGCGAAGGGCCTTGCCGCAAAGTGTGTAACGGAATA +GGTATTGGTGAATTTAAAGACTCACTCTCCATAAATGCTACGAATATTAAACACTTCAAA +AACTGCACCTCCATCAGTGGCGATCTCCACATCCTGCCGGTGGCATTTAGGGGTGACTCC +TTCACACATACTCCTCCTCTGGATCCACAGGAACTGGATATTCTGAAAACCGTAAAGGAA +ATCACAGGGTTTTTGCTGATTCAGGCTTGGCCTGAAAACAGGACGGACCTCCATGCCTTT +GAGAACCTAGAAATCATACGCGGCAGGACCAAGCAACATGGTCAGTTTTCTCTTGCAGTC +GTCAGCCTGAACATAACATCCTTGGGATTACGCTCCCTCAAGGAGATAAGTGATGGAGAT +GTGATAATTTCAGGAAACAAAAATTTGTGCTATGCAAATACAATAAACTGGAAAAAACTG +TTTGGGACCTCCGGTCAGAAAACCAAAATTATAAGCAACAGAGGTGAAAACAGCTGCAAG +GCCACAGGCCAGGTCTGCCATGCCTTGTGCTCCCCCGAGGGCTGCTGGGGCCCGGAGCCC +AGGGACTGCGTCTCTTGCCGGAATGTCAGCCGAGGCAGGGAATGCGTGGACAAGTGCAAG +CTTCTGGAGGGTGAGCCAAGGGAGTTTGTGGAGAACTCTGAGTGCATACAGTGCCACCCA +GAGTGCCTGCCTCAGGCCATGAACATCACCTGCACAGGACGGGGACCAGACAACTGTATC +CAGTGTGCCCACTACATTGACGGCCCCCACTGCGTCAAGACCTGCCCGGCAGGAGTCATG +GGAGAAAACAACACCCTGGTCTGGAAGTACGCAGACGCCGGCCATGTGTGCCACCTGTGC +CATCCAAACTGCACCTACGGATGCACTGGGCCAGGTCTTGAAGGCTGTCCAACGAATGGG +CCTAAGATCCCGTCCATCGCCACTGGGATGGTGGGGGCCCTCCTCTTGCTGCTGGTGGTG +GCCCTGGGGATCGGCCTCTTCATGCGAAGGCGCCACATCGTTCGGAAGCGCACGCTGCGG +AGGCTGCTGCAGGAGAGGGAGCTTGTGGAGCCTCTTACACCCAGTGGAGAAGCTCCCAAC +CAAGCTCTCTTGAGGATCTTGAAGGAAACTGAATTCAAAAAGATCAAAGTGCTGGGCTCC +GGTGCGTTCGGCACGGTGTATAAGGGACTCTGGATCCCAGAAGGTGAGAAAGTTAAAATT +CCCGTCGCTATCAAGGAATTAAGAGAAGCAACATCTCCGAAAGCCAACAAGGAAATCCTC +GATGAAGCCTACGTGATGGCCAGCGTGGACAACCCCCACGTGTGCCGCCTGCTGGGCATC +TGCCTCACCTCCACCGTGCAACTCATCACGCAGCTCATGCCCTTCGGCTGCCTCCTGGAC +TATGTCCGGGAACACAAAGACAATATTGGCTCCCAGTACCTGCTCAACTGGTGTGTGCAG +ATCGCAAAGGGCATGAACTACTTGGAGGACCGTCGCTTGGTGCACCGCGACCTGGCAGCC +AGGAACGTACTGGTGAAAACACCGCAGCATGTCAAGATCACAGATTTTGGGCTGGCCAAA +CTGCTGGGTGCGGAAGAGAAAGAATACCATGCAGAAGGAGGCAAAGTGCCTATCAAGTGG +ATGGCATTGGAATCAATTTTACACAGAATCTATACCCACCAGAGTGATGTCTGGAGCTAC +GGGGTGACCGTTTGGGAGTTGATGACCTTTGGATCCAAGCCATATGACGGAATCCCTGCC +AGCGAGATCTCCTCCATCCTGGAGAAAGGAGAACGCCTCCCTCAGCCACCCATATGTACC +ATCGATGTCTACATGATCATGGTCAAGTGCTGGATGATAGACGCAGATAGTCGCCCAAAG +TTCCGTGAGTTGATCATCGAATTCTCCAAAATGGCCCGAGACCCCCAGCGCTACCTTGTC +ATTCAGGGGGATGAAAGAATGCATTTGCCAAGTCCTACAGACTCCAACTTCTACCGTGCC +CTGATGGATGAAGAAGACATGGACGACGTGGTGGATGCCGACGAGTACCTCATCCCACAG +CAGGGCTTCTTCAGCAGCCCCTCCACGTCACGGACTCCCCTCCTGAGCTCTCTGAGTGCA +ACCAGCAACAATTCCACCGTGGCTTGCATTGATAGAAATGGGCTGCAAAGCTGTCCCATC +AAGGAAGACAGCTTCTTGCAGCGATACAGCTCAGACCCCACAGGCGCCTTGACTGAGGAC +AGCATAGACGACACCTTCCTCCCAGTGCCTGAATACATAAACCAGTCCGTTCCCAAAAGG +CCCGCTGGCTCTGTGCAGAATCCTGTCTATCACAATCAGCCTCTGAACCCCGCGCCCAGC +AGAGACCCACACTACCAGGACCCCCACAGCACTGCAGTGGGCAACCCCGAGTATCTCAAC +ACTGTCCAGCCCACCTGTGTCAACAGCACATTCGACAGCCCTGCCCACTGGGCCCAGAAA +GGCAGCCACCAAATTAGCCTGGACAACCCTGACTACCAGCAGGACTTCTTTCCCAAGGAA +GCCAAGCCAAATGGCATCTTTAAGGGCTCCACAGCTGAAAATGCAGAATACCTAAGGGTC +GCGCCACAAAGCAGTGAATTTATTGGAGCATGA + + + PF07714 + Pkinase_Tyr + + + PF00757 + Furin-like + + + PF01030 + Recep_L_domain + + + + + component + cell + + + component + membrane + + + function + nucleotide binding + + + function + ATP binding + + + function + purine nucleotide binding + + + function + transferase activity, transferring phosphorus-containing groups + + + function + adenyl nucleotide binding + + + function + kinase activity + + + function + binding + + + function + transferase activity + + + function + protein kinase activity + + + function + catalytic activity + + + function + transmembrane receptor protein tyrosine kinase activity + + + function + epidermal growth factor receptor activity + + + function + protein-tyrosine kinase activity + + + process + physiological process + + + process + protein amino acid phosphorylation + + + process + metabolism + + + process + cellular process + + + process + enzyme linked receptor protein signaling pathway + + + process + macromolecule metabolism + + + process + cell communication + + + process + transmembrane receptor protein tyrosine kinase signaling pathway + + + process + biopolymer metabolism + + + process + signal transduction + + + process + biopolymer modification + + + process + cell surface receptor linked signal transduction + + + process + protein modification + + + + + + BE0000901 + Low affinity immunoglobulin gamma Fc region receptor III-B + Human + + # Snyder LC, Astsaturov I, Weiner LM: Overview of monoclonal antibodies and small molecules targeting the epidermal growth factor receptor pathway in colorectal cancer. Clin Colorectal Cancer. 2005 Nov;5 Suppl 2:S71-80. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16336752 + unknown + + Low affinity immunoglobulin gamma Fc region receptor III-B + + Receptor for the Fc region of immunoglobulins gamma. Low affinity receptor. Binds complexed or aggregated IgG and also monomeric IgG. Contrary to III-A, is not capable to mediate antibody-dependent cytotoxicity and phagocytosis. May serve as a trap for immune complexes in the peripheral circulation which does not activate neutrophils + FCGR3B + 1q23 + Cell membrane; lipid-anchor; GPI-anchor. Secreted protein. Note=Secreted after cleavage + None + + 6.71 + 26216.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3620 + + + GenAtlas + FCGR3B + + + GeneCards + FCGR3B + + + GenBank Gene Database + X16863 + + + GenBank Protein Database + 31322 + + + UniProtKB + O75015 + + + UniProt Accession + FCG3B_HUMAN + + + + CD16b antigen + Fc-gamma RIII + Fc-gamma RIII-beta + Fc-gamma RIIIb + FcR-10 + FcRIII + FcRIIIb + IgG Fc receptor III-1 + Low affinity immunoglobulin gamma Fc region receptor III-B precursor + + >Low affinity immunoglobulin gamma Fc region receptor III-B precursor +MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQW +FHNESLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE +EDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKN +VSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI + >702 bp +ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT +GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGCGTGCTTGAGAAG +GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG +TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA +GTCAACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG +CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG +GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA +TATTTACAGAATGGCAAAGACAGGAAGTATTTTCATCATAATTCTGACTTCCACATTCCA +AAAGCCACACTCAAAGATAGCGGCTCCTACTTCTGCAGGGGGCTTGTTGGGAGTAAAAAT +GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA +TCATTCTCTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA +GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTTGA + + + PF00047 + ig + + + + + + + + BE0002093 + Complement C1r subcomponent + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Complement C1r subcomponent + + C1r B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system + C1R + 12p13 + Cytoplasmic + None + + 6.24 + 80174.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:1246 + + + GenAtlas + C1R + + + GeneCards + C1R + + + GenBank Gene Database + X04701 + + + GenBank Protein Database + 29539 + + + UniProtKB + P00736 + + + UniProt Accession + C1R_HUMAN + + + + Complement C1r subcomponent precursor + Complement component 1, r subcomponent + EC 3.4.21.41 + + >Complement C1r subcomponent +MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVF +QQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDF +SNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGY +ELQEDRHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPF +DIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKL +RYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQD +DGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSR +ESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVF +TNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRV +SVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVME +EKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAV +RDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED + >2118 bp +ATGTGGCTCTTGTACCTCCTGGTGCCGGCCCTGTTCTGCAGGGCAGGAGGCTCCATTCCC +ATCCCTCAGAAGTTATTTGGGGAGGTGACTTCCCCTCTGTTCCCCAAGCCTTACCCCAAC +AACTTTGAAACAACCACTGTGATCACAGTCCCCACGGGATACAGGGTGAAGCTCGTCTTC +CAGCAGTTTGACCTGGAGCCTTCTGAAGGCTGCTTCTATGATTATGTCAAGATCTCTGCT +GATAAGAAAAGCCTGGGGAGGTTCTGTGGGCAACTGGGTTCTCCACTGGGCAACCCCCCG +GGAAAGAAGGAATTTATGTCCCAAGGGAACAAGATGCTGCTGACCTTCCACACAGACTTC +TCCAACGAGGAGAATGGGACCATCATGTTCTACAAGGGCTTCCTGGCCTACTACCAAGCT +GTGGACCTTGATGAATGTGCTTCCCGGAGCAAATTAGGGGAGGAGGATCCCCAGCCCCAG +TGCCAGCACCTGTGTCACAACTACGTTGGAGGCTACTTCTGTTCCTGCCGTCCAGGCTAT +GAGCTTCAGGAAGACAGGCATTCCTGCCAGGCTGAGTGCAGCAGCGAGCTGTACACGGAG +GCATCAGGCTACATCTCCAGCCTGGAGTACCCTCGGTCCTACCCCCCTGACCTGCGCTGC +AACTACAGCATCCGGGTGGAGCGGGGCCTCACCCTGCACCTCAAGTTCCTGGAGCCTTTT +GATATTGATGACCACCAGCAAGTACACTGCCCCTATGACCAGCTACAGATCTATGCCAAC +GGGAAGAACATTGGCGAGTTCTGTGGGAAGCAAAGGCCCCCCGACCTCGACACCAGCAGC +AATGCTGTGGATCTGCTGTTCTTCACAGATGAGTCGGGGGACAGCCGGGGCTGGAAGCTG +CGCTACACCACCGAGATCATCAAGTGCCCCCAGCCCAAGACCCTAGACGAGTTCACCATC +ATCCAGAACCTGCAGCCTCAGTACCAGTTCCGTGACTACTTCATTGCTACCTGCAAGCAA +GGCTACCAGCTCATAGAGGGGAACCAGGTGCTGCATTCCTTCACAGCTGTCTGCCAGGAT +GATGGCACGTGGCATCGTGCCATGCCCAGATGCAAGATCAAGGACTGTGGGCAGCCCCGA +AACCTGCCTAATGGTGACTTCCGTTACACCACCACAATGGGAGTGAACACCTACAAGGCC +CGTATCCAGTACTACTGCCATGAGCCATATTACAAGATGCAGACCAGAGCTGGCAGCAGG +GAGTCTGAGCAAGGGGTGTACACCTGCACAGCACAGGGCATTTGGAAGAATGAACAGAAG +GGAGAGAAGATTCCTCGGTGCTTGCCAGTGTGTGGGAAGCCCGTGAACCCCGTGGAACAG +AGGCAGCGCATCATCGGAGGGCAAAAAGCCAAGATGGGCAACTTCCCCTGGCAGGTGTTC +ACCAACATCCACGGGCGCGGGGGCGGGGCCCTGCTGGGCGACCGCTGGATCCTCACAGCT +GCCCACACCCTGTATCCCAAGGAACACGAAGCGCAAAGCAACGCCTCTTTGGATGTGTTC +CTGGGCCACACAAATGTGGAAGAGCTCATGAAGCTAGGAAATCACCCCATCCGCAGGGTC +AGCGTCCACCCGGACTACCGTCAGGATGAGTCCTACAATTTTGAGGGGGACATCGCCCTG +CTGGAGCTGGAAAATAGTGTCACCCTGGGTCCCAACCTCCTCCCCATCTGCCTCCCTGAC +AACGATACCTTCTACGACCTGGGCTTGATGGGCTATGTCAGTGGCTTCGGGGTCATGGAG +GAGAAGATTGCTCATGACCTCAGGTTTGTCCGTCTGCCCGTAGCTAATCCACAGGCCTGT +GAGAACTGGCTCCGGGGAAAGAATAGGATGGATGTGTTCTCTCAAAACATGTTCTGTGCT +GGACACCCATCTCTAAAGCAGGACGCCTGCCAGGGGGATAGTGGGGGCGTTTTTGCAGTA +AGGGACCCGAACACTGATCGCTGGGTGGCCACGGGCATCGTGTCCTGGGGCATCGGGTGC +AGCAGGGGCTATGGCTTCTACACCAAAGTGCTCAACTACGTGGACTGGATCAAGAAAGAG +ATGGAGGAGGAGGACTGA + + + PF00089 + Trypsin + + + PF00084 + Sushi + + + PF07645 + EGF_CA + + + PF00431 + CUB + + + + + component + extracellular region + + + function + ion binding + + + function + cation binding + + + function + calcium ion binding + + + function + binding + + + function + peptidase activity + + + function + endopeptidase activity + + + function + catalytic activity + + + function + serine-type endopeptidase activity + + + function + hydrolase activity + + + process + response to biotic stimulus + + + process + defense response + + + process + protein metabolism + + + process + immune response + + + process + cellular protein metabolism + + + process + humoral immune response + + + process + complement activation + + + process + physiological process + + + process + metabolism + + + process + proteolysis + + + process + macromolecule metabolism + + + process + response to stimulus + + + + + + BE0002094 + Complement C1q subcomponent subunit A + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Complement C1q subcomponent subunit A + + C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes + C1QA + 1p36.12 + Secreted protein + None + + 9.45 + 26017.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:1241 + + + GenAtlas + C1QA + + + GeneCards + C1QA + + + GenBank Gene Database + AF135157 + + + GenBank Protein Database + 4894854 + + + UniProtKB + P02745 + + + UniProt Accession + C1QA_HUMAN + + + + Complement C1q subcomponent subunit A precursor + + >Complement C1q subcomponent subunit A +MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIR +TGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAI +RRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSR +GQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFL +IFPSA + >738 bp +ATGGAGGGTCCCCGGGGATGGCTGGTGCTCTGTGTGCTGGCCATATCGCTGGCCTCTATG +GTGACCGAGGACTTGTGCCGAGCACCAGACGGGAAGAAAGGGGAGGCAGGAAGACCTGGC +AGACGGGGGCGGCCAGGCCTCAAGGGGGAGCAAGGGGAGCCGGGGGCCCCTGGCATCCGG +ACAGGCATCCAAGGCCTTAAAGGAGACCAGGGGGAACCTGGGCCCTCTGGAAACCCCGGC +AAGGTGGGCTACCCAGGGCCCAGCGGCCCCCTCGGGGCCCGTGGCATCCCGGGAATTAAA +GGCACCAAGGGCAGCCCAGGAAACATCAAGGACCAGCCGAGGCCAGCCTTCTCCGCCATT +CGGCGGAACCCCCCAATGGGGGGCAACGTGGTCATCTTCGACACGGTCATCACCAACCAG +GAAGAACCGTACCAGAACCACTCCGGCCGATTCGTCTGCACTGTACCCGGCTACTACTAC +TTCACCTTCCAGGTGCTGTCCCAGTGGGAAATCTGCCTGTCCATCGTCTCCTCCTCAAGG +GGCCAGGTCCGACGCTCCCTGGGCTTCTGTGACACCACCAACAAGGGGCTCTTCCAGGTG +GTGTCAGGGGGCATGGTGCTTCAGCTGCAGCAGGGTGACCAGGTCTGGGTTGAAAAAGAC +CCCAAAAAGGGTCACATTTACCAGGGCTCTGAGGCCGACAGCGTCTTCAGCGGCTTCCTC +ATCTTCCCATCTGCCTGA + + + PF01391 + Collagen + + + PF00386 + C1q + + + + + component + cell + + + component + intracellular + + + component + cytoplasm + + + process + ion transport + + + process + anion transport + + + process + inorganic anion transport + + + process + phosphate transport + + + process + physiological process + + + process + cellular physiological process + + + process + transport + + + + + + BE0002095 + Complement C1q subcomponent subunit B + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Complement C1q subcomponent subunit B + + C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes + C1QB + 1p36.12 + Secreted protein + None + + 8.87 + 26460.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:1242 + + + GenAtlas + C1QB + + + GeneCards + C1QB + + + GenBank Gene Database + X03084 + + + GenBank Protein Database + 573114 + + + UniProtKB + P02746 + + + UniProt Accession + C1QB_HUMAN + + + + Complement C1q subcomponent subunit B precursor + + >Complement C1q subcomponent subunit B +MKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEK +GLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKI +AFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCV +NLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIF +SGFLLFPDMEA + >688 bp +CCAGGCCCAGCTCAGCTGCACCGGGCCCCCAGCCATCCCTGGCATCCCGGGTATCCCTGG +GACACCTGGCCCCGATGGCCAACCTGGGACCCCAGGGATAAAAGGAGAGAAAGGGCTTCC +AGGGCTGGCTGGAGACCATGGTGAGTTCGGAGAGAAGGGAGACCCAGGGATTCCTGGGAA +TCCAGGAAAAGTCGGCCCCAAGGGCCCCATGGGCCCTAAAGGTGGCCCAGGGGCCCCTGG +AGCCCCAGGCCCCAAAGGTGAATCGGGAGACTACAAGGCCACCCAGAAAATCGCCTTCTC +TGCCACAAGAACCATCAACGTCCCCCTGCGCCGGGACCAGACCATCCGCTTCGACCACGT +GATCACCAACATGAACAACAATTATGAGCCCCGCAGTGGCAAGTTCACCTGCAAGGTGCC +CGGTCTCTACTACTTCACCTACCACGCCAGCTCTCGAGGGAACCTGTGCGTGAACCTCAT +GCGTGGCCGGGAGCGTGCACAGAAGGTGGTCACCTTCTGTGACTATGCCTACAACACCTT +CCAGGTCACCACCGGTGGCATGGTCCTCAAGCTGGAGCAGGGGGAGAACGTCTTCCTGCA +GGCCACCGACAAGAACTCACTACTGGGCATGGAGGGTGCCAACAGCATCTTTTCCGGGTT +CCTGCTCTTTCCAGATATGGAGGCCTGA + + + PF01391 + Collagen + + + PF00386 + C1q + + + + + component + cell + + + component + intracellular + + + component + cytoplasm + + + process + anion transport + + + process + inorganic anion transport + + + process + phosphate transport + + + process + physiological process + + + process + cellular physiological process + + + process + transport + + + process + ion transport + + + + + + BE0002096 + Complement C1q subcomponent subunit C + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Complement C1q subcomponent subunit C + + C1q associates with the proenzymes C1r and C1s to yield C1, the first component of the serum complement system. The collagen-like regions of C1q interact with the Ca(2+)-dependent C1r(2)C1s(2) proenzyme complex, and efficient activation of C1 takes place on interaction of the globular heads of C1q with the Fc regions of IgG or IgM antibody present in immune complexes + C1QC + 1p36.11 + Secreted protein + None + + 8.58 + 25774.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:1245 + + + GenAtlas + C1QC + + + GeneCards + C1QC + + + GenBank Gene Database + AF087892 + + + GenBank Protein Database + 33150626 + + + UniProtKB + P02747 + + + UniProt Accession + C1QC_HUMAN + + + + Complement C1q subcomponent subunit C precursor + + >Complement C1q subcomponent subunit C +MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEP +GIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQS +VFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCV +LLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGF +LLFPD + >738 bp +ATGGACGTGGGGCCCAGCTCCCTGCCCCACCTTGGGCTGAAGCTGCTGCTGCTCCTGCTG +CTGCTGCCCCTCAGGGCCAAAGCCAACACAGGCTGCTACGGGATCCCAGGGATGCCCGGC +CTGCCCGGGGCACCAGGGAAGGATGGGTACGACGGACTGCCGGGGCCCAAGGGGGAGCCA +GGAATCCCAGCCATTCCCGGGATCCGAGGACCCAAAGGGCAGAAGGGAGAACCCGGCTTA +CCCGGCCATCCTGGGAAAAATGGCCCCATGGGACCCCCTGGGATGCCAGGGGTGCCCGGC +CCCATGGGATTCCCTGGAGAGCCAGGTGAGGAGGGCAGATACAAGCAGAAATTCCAGTCA +GTGTTCACGGTCACTCGGCAGACCCACCAGCCCCCTGCACCCAACAGCCTGATCAGATTC +AACGCGGTCCTCACCAACCCGCAGGAGGATTATGACACGAGCACTGGCAAGTTCACCTGC +AAAGTCCCCGGCCTCTACTACTTTGTCTACCACGCGTCGCATACAGCCAACCTGTGCGTG +CTGCTGTACCGCAGCGGCGTCAAAGTGGTCACCTTCTGTGGCCACACGTCCAAAACCAAT +CAGGTCAACTCGGGCGGTGTGCTGCTGAGGTTGCAGGTGGGCGAGGAGGTGTGGCTGGCT +GTCAATGACTACTACGACATGGTGGGCATCCAGGGCTCTGACAGCGTCTTCTCCGGCTTC +CTGCTCTTCCCCGACTAG + + + PF01391 + Collagen + + + PF00386 + C1q + + + + + component + cell + + + component + intracellular + + + component + cytoplasm + + + process + inorganic anion transport + + + process + phosphate transport + + + process + physiological process + + + process + cellular physiological process + + + process + transport + + + process + ion transport + + + process + anion transport + + + + + + BE0002097 + Low affinity immunoglobulin gamma Fc region receptor III-A + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 +# Zhang W, Gordon M, Schultheis AM, Yang DY, Nagashima F, Azuma M, Chang HM, Borucka E, Lurje G, Sherrod AE, Iqbal S, Groshen S, Lenz HJ: FCGR2A and FCGR3A polymorphisms associated with clinical outcome of epidermal growth factor receptor expressing metastatic colorectal cancer patients treated with single-agent cetuximab. J Clin Oncol. 2007 Aug 20;25(24):3712-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17704420 + unknown + + Low affinity immunoglobulin gamma Fc region receptor III-A + + Receptor for the Fc region of IgG. Binds complexed or aggregated IgG and also monomeric IgG. Mediates antibody-dependent cellular cytotoxicity (ADCC) and other antibody-dependent responses, such as phagocytosis + FCGR3A + 1q23 + Cell membrane + 209-229 + + 8.21 + 29089.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3619 + + + GenAtlas + FCGR3A + + + GeneCards + FCGR3A + + + GenBank Gene Database + X52645 + + + GenBank Protein Database + 31324 + + + UniProtKB + P08637 + + + UniProt Accession + FCG3A_HUMAN + + + + CD16a antigen + Fc-gamma RIII + Fc-gamma RIII-alpha + Fc-gamma RIIIa + FcR-10 + FcRIII + FcRIIIa + IgG Fc receptor III-2 + Low affinity immunoglobulin gamma Fc region receptor III-A precursor + + >Low affinity immunoglobulin gamma Fc region receptor III-A +MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQW +FHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE +EDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKN +VSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDW +KDHKFKWRKDPQDK + >765 bp +ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT +GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGGGTGCTCGAGAAG +GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG +TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA +GTCGACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG +CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG +GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA +TATTTACAGAATGGCAAAGGCAGGAAGTATTTTCATCATAATTCTGACTTCTACATTCCA +AAAGCCACACTCAAAGACAGCGGCTCCTACTTCTGCAGGGGGCTTTTTGGGAGTAAAAAT +GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA +TCATTCTTTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA +GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTCGAAGCTCAACAAGAGACTGG +AAGGACCATAAATTTAAATGGAGAAAGGACCCTCAAGACAAATGA + + + PF00047 + ig + + + + + + + + BE0001529 + Complement C1s subcomponent + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Complement C1s subcomponent + Involved in calcium ion binding + C1s B chain is a serine protease that combines with C1q and C1s to form C1, the first component of the classical pathway of the complement system. C1r activates C1s so that it can, in turn, activate C2 and C4 + C1S + 12p13 + Cytoplasmic + None + + 4.59 + 76685.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:1247 + + + GenAtlas + C1S + + + GeneCards + C1S + + + GenBank Gene Database + X06596 + + + GenBank Protein Database + 763110 + + + UniProtKB + P09871 + + + UniProt Accession + C1S_HUMAN + + + + C1 esterase + Complement C1s subcomponent precursor + EC 3.4.21.42 + + >Complement C1s subcomponent precursor +MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIE +LSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERF +TGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVF +TALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVF +VAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTP +NSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCG +IPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPK +CVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGN +REPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVK +MGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKV +EKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCG +TYGLYTRVKNYVDWIMKTMQENSTPRED + >2067 bp +ATGTGGTGCATTGTCCTGTTTTCACTTTTGGCATGGGTTTATGCTGAGCCTACCATGTAT +GGGGAGATCCTGTCCCCTAACTATCCTCAGGCATATCCCAGTGAGGTAGAGAAATCTTGG +GACATAGAAGTTCCTGAAGGGTATGGGATTCACCTCTACTTCACCCATCTGGACATTGAG +CTGTCAGAGAACTGTGCGTATGACTCAGTGCAGATAATCTCAGGAGACACTGAAGAAGGG +AGGCTCTGTGGACAGAGGAGCAGTAACAATCCCCACTCTCCAATTGTGGAAGAGTTCCAA +GTCCCATACAACAAACTCCAGGTGATCTTTAAGTCAGACTTTTCCAATGAAGAGCGTTTT +ACGGGGTTTGCTGCATACTATGTTGCCACAGACATAAATGAATGCACAGATTTTGTAGAT +GTCCCTTGTAGCCACTTCTGCAACAATTTCATTGGTGGTTACTTCTGCTCCTGCCCCCCG +GAATATTTCCTCCATGATGACATGAAGAATTGCGGAGTTAATTGCAGTGGGGATGTATTC +ACTGCACTGATTGGGGAGATTGCAAGTCCCAATTATCCCAAACCATATCCAGAGAACTCA +AGGTGTGAATACCAGATCCGGTTGGAGAAAGGGTTCCAAGTGGTGGTGACCTTGCGGAGA +GAAGATTTTGATGTGGAAGCAGCTGACTCAGCGGGAAACTGCCTTGACAGTTTAGTTTTT +GTTGCAGGAGATCGGCAATTTGGTCCTTACTGTGGTCATGGATTCCCTGGGCCTCTAAAT +ATTGAAACCAAGAGTAATGCTCTTGATATCATCTTCCAAACTGATCTAACAGGGCAAAAA +AAGGGCTGGAAACTTCGCTATCATGGAGATCCAATGCCCTGCCCTAAGGAAGACACTCCC +AATTCTGTTTGGGAGCCTGCGAAGGCAAAATATGTCTTTAGAGATGTGGTGCAGATAACC +TGTCTGGATGGGTTTGAAGTTGTGGAGGGACGTGTTGGTGCAACATCTTTCTATTCGACT +TGTCAAAGCAATGGAAAGTGGAGTAATTCCAAACTGAAATGTCAACCTGTGGACTGTGGC +ATTCCTGAATCCATTGAGAATGGTAAAGTTGAAGACCCAGAGAGCACTTTGTTTGGTTCT +GTCATCCGCTACACTTGTGAGGAGCCATATTACTACATGGAAAATGGAGGAGGTGGGGAG +TATCACTGTGCTGGTAACGGGAGCTGGGTGAATGAGGTGCTGGGCCCGGAGCTGCCGAAA +TGTGTTCCAGTCTGTGGAGTCCCCAGAGAACCCTTTGAAGAAAAACAGAGGATAATTGGA +GGATCCGATGCAGATATTAAAAACTTCCCCTGGCAAGTCTTCTTTGACAACCCATGGGCT +GGTGGAGCGCTCATTAATGAGTACTGGGTGCTGACGGCTGCTCATGTTGTGGAGGGAAAC +AGGGAGCCAACAATGTATGTTGGGTCCACCTCAGTGCAGACCTCACGGCTGGCAAAATCC +AAGATGCTCACTCCTGAGCATGTGTTTATTCATCCGGGATGGAAGCTGCTGGAAGTCCCA +GAAGGACGAACCAATTTTGATAATGACATTGCACTGGTGCGGCTGAAAGACCCAGTGAAA +ATGGGACCCACCGTCTCTCCCATCTGCCTACCAGGCACCTCTTCCGACTACAACCTCATG +GATGGGGACCTGGGACTGATCTCAGGCTGGGGCCGAACAGAGAAGAGAGATCGTGCTGTT +CGCCTCAAGGCGGCAAGGTTACCTGTAGCTCCTTTAAGAAAATGCAAAGAAGTGAAAGTG +GAGAAACCCACAGCAGATGCAGAGGCCTATGTTTTCACTCCTAACATGATCTGTGCTGGA +GGAGAGAAGGGCATGGATAGCTGTAAAGGGGACAGTGGTGGGGCCTTTGCTGTACAGGAT +CCCAATGACAAGACCAAATTCTACGCAGCTGGCCTGGTGTCCTGGGGGCCCCAGTGTGGG +ACCTATGGGCTCTACACACGGGTAAAGAACTATGTTGACTGGATAATGAAGACTATGCAG +GAAAATAGCACCCCCCGTGAGGACTAA + + + PF00008 + EGF + + + PF00089 + Trypsin + + + PF00084 + Sushi + + + PF00431 + CUB + + + + + component + extracellular region + + + function + endopeptidase activity + + + function + catalytic activity + + + function + serine-type endopeptidase activity + + + function + hydrolase activity + + + function + ion binding + + + function + cation binding + + + function + calcium ion binding + + + function + binding + + + function + peptidase activity + + + process + metabolism + + + process + proteolysis + + + process + macromolecule metabolism + + + process + response to stimulus + + + process + response to biotic stimulus + + + process + defense response + + + process + protein metabolism + + + process + immune response + + + process + cellular protein metabolism + + + process + humoral immune response + + + process + complement activation + + + process + physiological process + + + + + + BE0000710 + High affinity immunoglobulin gamma Fc receptor I + Human + + # Negri DR, Tosi E, Valota O, Ferrini S, Cambiaggi A, Sforzini S, Silvani A, Ruffini PA, Colnaghi MI, Canevari S: In vitro and in vivo stability and anti-tumour efficacy of an anti-EGFR/anti-CD3 F(ab')2 bispecific monoclonal antibody. Br J Cancer. 1995 Oct;72(4):928-33. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/7547242 + unknown + + High affinity immunoglobulin gamma Fc receptor I + Involved in receptor signaling protein activity + Binds to the Fc region of immunoglobulins gamma. High affinity receptor + FCGR1A + 1q21.2-q21.3 + Membrane; single-pass type I membrane protein + 293-313 + + 8.08 + 42632.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3613 + + + GenAtlas + FCGR1A + + + GeneCards + FCGR1A + + + GenBank Gene Database + X14356 + + + GenBank Protein Database + 31332 + + + UniProtKB + P12314 + + + UniProt Accession + FCGR1_HUMAN + + + + CD64 antigen + Fc-gamma RI + FcRI + High affinity immunoglobulin gamma Fc receptor I precursor + IgG Fc receptor I + + >High affinity immunoglobulin gamma Fc receptor I precursor +MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNG +TATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPL +ALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAG +ISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRN +TSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVG +IMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQ +LQEGVHRKEPQGAT + >1125 bp +ATGTGGTTCTTGACAACTCTGCTCCTTTGGGTTCCAGTTGATGGGCAAGTGGACACCACA +AAGGCAGTGATCTCTTTGCAGCCTCCATGGGTCAGCGTGTTCCAAGAGGAAACCGTAACC +TTGCACTGTGAGGTGCTCCATCTGCCTGGGAGCAGCTCTACACAGTGGTTTCTCAATGGC +ACAGCCACTCAGACCTCGACCCCCAGCTACAGAATCACCTCTGCCAGTGTCAATGACAGT +GGTGAATACAGGTGCCAGAGAGGTCTCTCAGGGCGAAGTGACCCCATACAGCTGGAAATC +CACAGAGGCTGGCTACTACTGCAGGTCTCCAGCAGAGTCTTCACGGAAGGAGAACCTCTG +GCCTTGAGGTGTCATGCGTGGAAGGATAAGCTGGTGTACAATGTGCTTTACTATCGAAAT +GGCAAAGCCTTTAAGTTTTTCCACTGGAATTCTAACCTCACCATTCTGAAAACCAACATA +AGTCACAATGGCACCTACCATTGCTCAGGCATGGGAAAGCATCGCTACACATCAGCAGGA +ATATCTGTCACTGTGAAAGAGCTATTTCCAGCTCCAGTGCTGAATGCATCTGTGACATCC +CCACTCCTGGAGGGGAATCTGGTCACCCTGAGCTGTGAAACAAAGTTGCTCTTGCAGAGG +CCTGGTTTGCAGCTTTACTTCTCCTTCTACATGGGCAGCAAGACCCTGCGAGGCAGGAAC +ACATCCTCTGAATACCAAATACTAACTGCTAGAAGAGAAGACTCTGGGTTATACTGGTGC +GAGGCTGCCACAGAGGATGGAAATGTCCTTAAGCGCAGCCCTGAGTTGGAGCTTCAAGTG +CTTGGCCTCCAGTTACCAACTCCTGTCTGGTTTCATGTCCTTTTCTATCTGGCAGTGGGA +ATAATGTTTTTAGTGAACACTGTTCTCTGGGTGACAATACGTAAAGAACTGAAAAGAAAG +AAAAAGTGGGATTTAGAAATCTCTTTGGATTCTGGTCATGAGAAGAAGGTAACTTCCAGC +CTTCAAGAAGACAGACATTTAGAAGAAGAGCTGAAATGTCAGGAACAAAAAGAAGAACAG +CTGCAGGAAGGGGTGCACCGGAAGGAGCCCCAGGGGGCCACGTAG + + + PF00047 + ig + + + + + + + + BE0002098 + Low affinity immunoglobulin gamma Fc region receptor II-a + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 +# Zhang W, Gordon M, Schultheis AM, Yang DY, Nagashima F, Azuma M, Chang HM, Borucka E, Lurje G, Sherrod AE, Iqbal S, Groshen S, Lenz HJ: FCGR2A and FCGR3A polymorphisms associated with clinical outcome of epidermal growth factor receptor expressing metastatic colorectal cancer patients treated with single-agent cetuximab. J Clin Oncol. 2007 Aug 20;25(24):3712-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17704420 + unknown + + Low affinity immunoglobulin gamma Fc region receptor II-a + + Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens + FCGR2A + 1q23 + Membrane + 218-240 + + 6.78 + 34990.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3616 + + + GenAtlas + FCGR2A + + + GeneCards + FCGR2A + + + GenBank Gene Database + M31932 + + + GenBank Protein Database + 182474 + + + UniProtKB + P12318 + + + UniProt Accession + FCG2A_HUMAN + + + + CD32 antigen + CDw32 + Fc-gamma RII-a + Fc-gamma-RIIa + FcRII-a + IgG Fc receptor II-a + Low affinity immunoglobulin gamma Fc region receptor II-a precursor + + >Low affinity immunoglobulin gamma Fc region receptor II-a +MAMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTL +TCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVL +SEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSRLDPTFSIPQANHS +HSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIY +CRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDD +KNIYLTLPPNDHVNSNN + >954 bp +ATGGCTATGGAGACCCAAATGTCTCAGAATGTATGTCCCAGAAACCTGTGGCTGCTTCAA +CCATTGACAGTTTTGCTGCTGCTGGCTTCTGCAGACAGTCAAGCTGCAGCTCCCCCAAAG +GCTGTGCTGAAACTTGAGCCCCCGTGGATCAACGTGCTCCAGGAGGACTCTGTGACTCTG +ACATGCCAGGGGGCTCGCAGCCCTGAGAGCGACTCCATTCAGTGGTTCCACAATGGGAAT +CTCATTCCCACCCACACGCAGCCCAGCTACAGGTTCAAGGCCAACAACAATGACAGCGGG +GAGTACACGTGCCAGACTGGCCAGACCAGCCTCAGCGACCCTGTGCATCTGACTGTGCTT +TCCGAATGGCTGGTGCTCCAGACCCCTCACCTGGAGTTCCAGGAGGGAGAAACCATCATG +CTGAGGTGCCACAGCTGGAAGGACAAGCCTCTGGTCAAGGTCACATTCTTCCAGAATGGA +AAATCCCAGAAATTCTCCCGTTTGGATCCCACCTTCTCCATCCCACAAGCAAACCACAGT +CACAGTGGTGATTACCACTGCACAGGAAACATAGGCTACACGCTGTTCTCATCCAAGCCT +GTGACCATCACTGTCCAAGTGCCCAGCATGGGCAGCTCTTCACCAATGGGGATCATTGTG +GCTGTGGTCATTGCGACTGCTGTAGCAGCCATTGTTGCTGCTGTAGTGGCCTTGATCTAC +TGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTGAAGGCTGCCCAATTTGAG +CCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACTTGAAGAAACCAACAATGAC +TATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGGGCACCTACTGACGATGAT +AAAAACATCTACCTGACTCTTCCTCCCAACGACCATGTCAACAGTAATAACTAA + + + PF00047 + ig + + + + + + + + BE0002099 + Low affinity immunoglobulin gamma Fc region receptor II-b + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Low affinity immunoglobulin gamma Fc region receptor II-b + + Receptor for the Fc region of complexed or aggregated immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B- cells. Binding to this receptor results in down-modulation of previous state of cell activation triggered via antigen receptors on B-cells (BCR), T-cells (TCR) or via another Fc receptor. Isoform IIB1 fails to mediate endocytosis or phagocytosis. Isoform IIB2 does not trigger phagocytosis + FCGR2B + 1q23 + Membrane + 218-240 + + 6.12 + 34044.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:3618 + + + GenAtlas + FCGR2B + + + GeneCards + FCGR2B + + + GenBank Gene Database + U87560 + + + GenBank Protein Database + 4099445 + + + UniProtKB + P31994 + + + UniProt Accession + FCG2B_HUMAN + + + + CD32 antigen + CDw32 + Fc-gamma RII-b + Fc-gamma-RIIb + FcRII-b + IgG Fc receptor II-b + Low affinity immunoglobulin gamma Fc region receptor II-b precursor + + >Low affinity immunoglobulin gamma Fc region receptor II-b +MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN +VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL +SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN +FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA +VVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDA +LEEPDDQNRI + >930 bp +ATGGGAATCCTGTCATTCTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG +TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT +GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC +GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC +TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG +TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC +AGCGACCCTGTGCATCTGACTGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG +GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG +GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC +TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCACTGCACAGGAAACATA +GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA +CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCGGCCATTGTTGCTGCT +GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCTCTCCCAGGATACCCTGAG +TGCAGGGAAATGGGAGAGACCCTCCCTGAGAAACCAGCCAATCCCACTAATCCTGATGAG +GCTGACAAAGTTGGGGCTGAGAACACAATCACCTATTCACTTCTCATGCACCCGGATGCT +CTGGAAGAGCCTGATGACCAGAACCGTATT + + + PF00047 + ig + + + + + + + + BE0002100 + Low affinity immunoglobulin gamma Fc region receptor II-c + Human + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 + unknown + + Low affinity immunoglobulin gamma Fc region receptor II-c + + Receptor for the Fc region of complexed immunoglobulins gamma. Low affinity receptor. Involved in a variety of effector and regulatory functions such as phagocytosis of immune complexes and modulation of antibody production by B-cells + FCGR2C + 1q23.3 + Cell membrane + 224-246 + + 6.9 + 35578.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:15626 + + + GenAtlas + FCGR2C + + + GeneCards + FCGR2C + + + GenBank Gene Database + X17652 + + + GenBank Protein Database + 32074 + + + UniProtKB + P31995 + + + UniProt Accession + FCG2C_HUMAN + + + + CD32 antigen + CDw32 + Fc-gamma RII-c + Fc-gamma-RIIc + FcRII-c + IgG Fc receptor II-c + Low affinity immunoglobulin gamma Fc region receptor II-c precursor + + >Low affinity immunoglobulin gamma Fc region receptor II-c +MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN +VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL +SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN +FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA +VVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQPEETNNDYETADGGYMTLNPR +APTDDDKNIYLTLPPNDHVNSNN + >972 bp +ATGGGAATCCTGTCATTTTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG +TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT +GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC +GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC +TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG +TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC +AGCGACCCTGTGCATCTGACAGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG +GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG +GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC +TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCATTGCACAGGAAACATA +GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA +CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCTGCCATTGTTGCTGCT +GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTG +AAGGCTGCCCAATTTGAGCCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACCT +GAAGAAACCAACAATGACTATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGG +GCACCTACTGACGATGATAAAAACATCTACTTGACTCTTCCTCCCAACGACCATGTCAAC +AGTAATAACTAA + + + PF00047 + ig + + + + + + + + + + + + + DB00003 + BIOD00001 + BTD00001 + Dornase alfa + Dornase alfa is a biosynthetic form of human deoxyribunuclease I (DNase I) enzyme. It is produced in genetically modified Chinese hamster ovary (CHO) cells using recombinant DNA technology. The 260-amino acid sequence of dornase alfa is identical to the endogenous human enzyme. Dornase alfa cleaves extracellular DNA to 5´-phosphodinucleotide and 5´-phosphooligonucleotide end products without affecting intracellular DNA. In individuals with cystic fibrosis, extracellular DNA, which is an extremely viscous anion, is released by degenerating leukocytes that accumulate during inflammatory responses to infections. Enzymatic breakdown of this extracellular DNA appears to reduce sputum viscosity and viscoelasticity. + 9003-98-9 + + approved + + # Cramer GW, Bosso JA: The role of dornase alfa in the treatment of cystic fibrosis. Ann Pharmacother. 1996 Jun;30(6):656-61. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/8792953 +# Jones AP, Wallis C: Dornase alfa for cystic fibrosis. Cochrane Database Syst Rev. 2010 Mar 17;3:CD001127. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/20238314 +# Riethmueller J, Kumpf M, Borth-Bruhns T, Brehm W, Wiskirchen J, Sieverding L, Ankele C, Hofbeck M, Baden W: Clinical and in vitro effect of dornase alfa in mechanically ventilated pediatric non-cystic fibrosis patients with atelectases. Cell Physiol Biochem. 2009;23(1-3):205-10. Epub 2009 Feb 18. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/19255515 +# Roche Products Limited. Pulmozyme. 1st ed. Newmarket, Auckland: N.p., 2014. Web. 11 Nov. 2014. +#Glowm.com,. 'Dornase Alfa'. N.p., 2014. Web. 11 Nov. 2014. + + Used as adjunct therapy in the treatment of cystic fibrosis. + Cystic fibrosis (CF) is a disease characterized by the retention of viscous purulent secretions in the airways. These thick secretions contribute both to reduced pulmonary function and to frequent pulmonary infection. Purulent pulmonary secretions of individuals with cystic fibrosis contain very high concentrations of extracellular DNA released by degenerating leukocytes that accumulate in response to these infections. Dornase alfa hydrolyzes the DNA in sputum of CF patients and reduces sputum viscosity and viscoelasticity. The enzyme does not appear to affect sputum in the absence of an inflammatory response to infection, nor does it affect the sputum of healthy individuals. + Dornase alfa is a biosynthetic form of human DNase I. The enzyme is involved in endonucleolytic cleavage of extracellular DNA to 5´-phosphodinucleotide and 5´-phosphooligonucleotide end products. It has no effect on intracellular DNA. Optimal activity is dependent on the presence of divalent cations such as calcium and magnesium. Extracellular DNA is a viscous anionic polymer and its breakdown appears to improve the viscosity and viscoelasticity of purulent sputum of individuals with CF, thus reducing airflow obstruction. Dornase alfa does not seem to have any effect on non-purulent sputum. + Adverse reactions occur at a frequency of < 1/1000 and are usually mild and transient in nature. Reported adverse effects include chest pain (pleuritic/non-cardiac), fever, dyspepsia, voice alteration (hoarseness), pharyngitis, dyspnea, laryngitis, rhinitis, decreased lung function, rash, urticaria, and conjunctivitis. There is no evidence of carcinogenic or mutagenic properties. The safety of dornase alfa has not been studied in pregnant women, nursing women and children under the age of 5 years old. + While no conclusive studies have yet been published, dornase alfa is expected to be metabolized by proteases in biofluids. + Studies in rats and monkeys after inhalation of dornase alfa shows very little systemic absorption (less than 15% for rats and less than 2% for monkeys). The results were also witnessed in patients. Dornase alfa is also associated with very low accumulation with no serum concentration greater than 10ng/mL observed no matter the dose administered. Bioavailability: mean sputum concentrations of dornase alfa can be measured after 15 minutes. Onset is achieved within 3 to 7 days. Peak concentrations are achieved after 9 days. + + + + In studies in rats and monkeys, the initial volume of distribution is similar to the serum volume. Concentrations in sputum decline rapidly after inhalation. + Studies in rats indicate that, following aerosol administration, the disappearance half-life of dornase alfa from the lungs is 11 hours. In humans, sputum DNase levels declined below half of those detected immediately post-administration within 2 hours but effects on sputum rheology persisted beyond 12 hours. + + + Peptides + Organic Compounds + Organic Acids + Carboxylic Acids and Derivatives + Amino Acids, Peptides, and Analogues + + + + Deoxyribonuclease I + Deoxyribonuclease-1 precursor + DNase + DNase I + rhDNase + + + + Pulmozyme + 50242-100_1f306717-b937-4efc-a269-bcadda447cce + 50242-100 + 1993-12-30 + + solution + 1 mg/mL + respiratory (inhalation) + BLA103532 + false + false + true + US + FDA NDC + + + + Viscozyme + + + + Cauterex + dornase alfa + fibrinolysin + gentamicin sulfate + + + Clorfibrase + dornase alfa + fibrinolysin + chloramphenicol + + + Elase + dornase alfa + fibrinolysin + + + Fibrabene + dornase alfa + fibrinolysin (bovine) + + + Fibrase SA + dornase alfa + fibrinolysin (bovine) + + + Fibrolan + dornase alfa + fibrinolysin (bovine) + + + Parkelase + dornase alfa + fibrinolysin + + + Ridasa + dornase alfa + ribonuclease + + + + + Cardinal Health + http://www.cardinal.com + + + Catalent Pharma Solutions + http://www.catalent.com + + + F Hoffmann-La Roche Ltd. + http://www.roche.com + + + Genentech Inc. + http://www.gene.com + + + Meda AB + http://www.meda.se + + + Medpointe Pharmaceuticals + + + + + Genentech, Inc + + + + Lufyllin 200 mg tablet + 3.21 + tablet + + + Lufyllin-gg tablet + 3.84 + tablet + + + Lufyllin-GG 200-200 mg tablet + 3.99 + tablet + + + Lufyllin-400 tablet + 4.62 + tablet + + + Lufyllin 400 mg tablet + 4.81 + tablet + + + Pulmozyme 1 mg/ml ampul + 37.05 + ml + + + Pulmozyme 1 mg/ml Solution 2.5ml Plastic Container + 77.06 + plastic + + + Lufyllin-GG 100-100 mg/15ml Elixir + 0.6 + ml + + + + + Enzymes + + + + + Humans and other mammals + + + +
Solution
+ respiratory (inhalation) + 1 mg/mL +
+
+ + + RESPIRATORY SYSTEM + COUGH AND COLD PREPARATIONS + EXPECTORANTS, EXCL. COMBINATIONS WITH COUGH SUPPRESSANTS + Mucolytics + + + + 44:00 + + + + 2137237 + Canada + 2004-10-26 + 2013-05-28 + + + 2184581 + Canada + 2005-02-22 + 2015-02-28 + + + + + + >Dornase alfa sequence +LKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAP +DTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFS +RFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQ +WSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYG +LSDQLAQAISDHYPVEVMLK + + + + Melting Point + 67 °C + Chan, H.K. et al., Pharm Res. 13:756-761 (1996) + + + Hydrophobicity + -0.083 + + + + Isoelectric Point + 4.58 + + + + Molecular Weight + 29253.9000 + + + + Molecular Formula + C1321H1999N339O396S9 + + + + + + GenBank + M55983 + + + PharmGKB + PA10318 + + + UniProtKB + P24855 + + + Wikipedia + Dornase_alfa + + + + + RxList + http://www.rxlist.com/cgi/generic/pulmozyme.htm + + + Drugs.com + http://www.drugs.com/cdi/dornase-alfa.html + + + + + + + + + BE0004796 + DNA + Human + + # Cramer GW, Bosso JA: The role of dornase alfa in the treatment of cystic fibrosis. Ann Pharmacother. 1996 Jun;30(6):656-61. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/8792953 + yes + + + + + +
+ + DB00004 + BIOD00084 + BTD00084 + Denileukin diftitox + A recombinant DNA-derived cytotoxic protein composed of the amino acid sequences for diphtheria toxin fragments A and B (Met 1-Thr 387)-His followed by the sequences for interleukin-2 (IL-2; Ala 1-Thr 133). It is produced in an E. coli expression system. + 173146-27-5 + + approved + investigational + + # Turturro F: Denileukin diftitox: a biotherapeutic paradigm shift in the treatment of lymphoid-derived disorders. Expert Rev Anticancer Ther. 2007 Jan;7(1):11-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17187516 +# Park M, Liu GT, Piltz-Seymour J, Wisda CL, Rook AH, Junkins-Hopkins JM, Nasta SD, Kim EJ: Vision loss following denileukin diftitox treatment: a case report of possible posterior ischemic optic neuropathy. Leuk Lymphoma. 2007 Apr;48(4):808-11. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17454642 + + For treatment of cutaneous T-cell lymphoma + Denileukin diftitox (Ontak) directs the cytocidal action of diphtheria toxin to cells which express the IL-2 receptor. The human IL-2 receptor exists in three forms, low (CD25), intermediate (CD122/CD132) and high (CD25/CD122/CD132) affinity. Malignant cells expressing one or more of the subunits of the IL-2 receptor are found in certain leukemias and lymphomas including cutaneous T-cell lymphoma (CTCL). Ontak interacts with the high affinity IL-2 receptor on the cell surface and inhibits cellular protein synthesis, resulting in cell death within hours. + Denileukin diftitox binds to the high-affinity IL-2 receptor complex. The IL-2 receptor (Tac) subunit is expressed on activated but not resting lymphocytes. The diphtheria toxin associated with Ontak then selectively kills the IL-2 bearing cells. + + + + 70-80 min + + + * 0.06 to 0.09 L/kg + * 0.6 - 2.0 mL/min/kg [Lymphoma] + + + Peptides + Organic Compounds + Organic Acids + Carboxylic Acids and Derivatives + Amino Acids, Peptides, and Analogues + + + + Diphtheria toxin precursor + DT + NAD(+--diphthamide ADP- ribosyltransferase) + + + + Ontak + 62856-603_f2eba925-c3a4-45db-a391-23e7a11bdb24 + 62856-603 + 2008-10-15 + + injection, solution + 150 ug/mL + intravenous + BLA103767 + false + false + true + US + FDA NDC + + + + + + + Eisai Inc. + http://www.eisai.com + + + Hollister-Stier Laboratories LLC + http://www.hollisterstier.com + + + Ligand Pharmaceuticals Inc. + http://www.ligand.com + + + + + + Ontak 150 mcg/ml vial + 878.4 + ml + + + + + Antineoplastic Agents + + + + + Humans and other mammals + + + +
Injection, solution
+ intravenous + 150 ug/mL +
+
+ + + ANTINEOPLASTIC AND IMMUNOMODULATING AGENTS + ANTINEOPLASTIC AGENTS + OTHER ANTINEOPLASTIC AGENTS + Other antineoplastic agents + + + + + + + + DB06372 + Rilonacept + decreases effects of toxoids by pharmacodynamic antagonism. + + + DB00072 + Trastuzumab + Trastuzumab may increase the risk of neutropenia and anemia. Monitor closely for signs and symptoms of adverse events. + + + + >DB00004 sequence +MGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNK +YDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVG +TEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMY +EYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVS +EEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEK +TTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYN +FVESIINLFQVVHNSYNRPAYSPGHKTHAPTSSSTKKTQLQLEHLLLDLQMILNGINNYK +NPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVI +VLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT + + + + Hydrophobicity + -0.301 + + + + Isoelectric Point + 5.45 + + + + Molecular Weight + 57647.3000 + + + + Molecular Formula + C2560H4042N678O799S17 + + + + + + National Drug Code Directory + 62856-603-01 + + + GenBank + V01536 + + + PharmGKB + PA164750594 + + + UniProtKB + P00587 + + + Wikipedia + Denileukin_diftitox + + + + + RxList + http://www.rxlist.com/cgi/generic2/denileukin.htm + + + Drugs.com + http://www.drugs.com/cdi/denileukin-diftitox.html + + + + + + + + + BE0000658 + Interleukin-2 receptor subunit alpha + Human + + binder + + # Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17139284 +# 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":http://www.ncbi.nlm.nih.gov/pubmed/17016423 +# Kiyokawa T, Shirono K, Hattori T, Nishimura H, Yamaguchi K, Nichols JC, Strom TB, Murphy JR, Takatsuki K: Cytotoxicity of interleukin 2-toxin toward lymphocytes from patients with adult T-cell leukemia. Cancer Res. 1989 Jul 15;49(14):4042-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/2786749 +# Murphy JR, Kelley VE, Strom TB: Interleukin 2 toxin: a step toward selective immunomodulation. Am J Kidney Dis. 1988 Feb;11(2):159-62. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/3124610 +# Duvic M, Talpur R: Optimizing denileukin diftitox (Ontak) therapy. Future Oncol. 2008 Aug;4(4):457-69. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/18684057 +# Turturro F: Denileukin diftitox: a biotherapeutic paradigm shift in the treatment of lymphoid-derived disorders. Expert Rev Anticancer Ther. 2007 Jan;7(1):11-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17187516 +# Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11752352 + yes + + Interleukin-2 receptor subunit alpha + Involved in interleukin-2 receptor activity + Receptor for interleukin-2 + IL2RA + 10p15-p14 + Membrane; single-pass type I membrane protein + 241-259 + + 6.49 + 30819.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:6008 + + + GenAtlas + IL2RA + + + GeneCards + IL2RA + + + GenBank Gene Database + X01057 + + + GenBank Protein Database + 33813 + + + UniProtKB + P01589 + + + UniProt Accession + IL2RA_HUMAN + + + + CD25 antigen + IL-2 receptor alpha subunit + IL-2-RA + IL2-RA + Interleukin-2 receptor alpha chain precursor + p55 + TAC antigen + + >Interleukin-2 receptor alpha chain precursor +MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKS +GSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQAS +LPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQP +QLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQ +VAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI + >819 bp +ATGGATTCATACCTGCTGATGTGGGGACTGCTCACGTTCATCATGGTGCCTGGCTGCCAG +GCAGAGCTCTGTGACGATGACCCGCCAGAGATCCCACACGCCACATTCAAAGCCATGGCC +TACAAGGAAGGAACCATGTTGAACTGTGAATGCAAGAGAGGTTTCCGCAGAATAAAAAGC +GGGTCACTCTATATGCTCTGTACAGGAAACTCTAGCCACTCGTCCTGGGACAACCAATGT +CAATGCACAAGCTCTGCCACTCGGAACACAACGAAACAAGTGACACCTCAACCTGAAGAA +CAGAAAGAAAGGAAAACCACAGAAATGCAAAGTCCAATGCAGCCAGTGGACCAAGCGAGC +CTTCCAGGTCACTGCAGGGAACCTCCACCATGGGAAAATGAAGCCACAGAGAGAATTTAT +CATTTCGTGGTGGGGCAGATGGTTTATTATCAGTGCGTCCAGGGATACAGGGCTCTACAC +AGAGGTCCTGCTGAGAGCGTCTGCAAAATGACCCACGGGAAGACAAGGTGGACCCAGCCC +CAGCTCATATGCACAGGTGAAATGGAGACCAGTCAGTTTCCAGGTGAAGAGAAGCCTCAG +GCAAGCCCCGAAGGCCGTCCTGAGAGTGAGACTTCCTGCCTCGTCACAACAACAGATTTT +CAAATACAGACAGAAATGGCTGCAACCATGGAGACGTCCATATTTACAACAGAGTACCAG +GTAGCAGTGGCCGGCTGTGTTTTCCTGCTGATCAGCGTCCTCCTCCTGAGTGGGCTCACC +TGGCAGCGGAGACAGAGGAAGAGTAGAAGAACAATCTAG + + + PF00084 + Sushi + + + + + + + + BE0000651 + Interleukin-2 receptor subunit beta + Human + + agonist + + # Foss F, Demierre MF, DiVenuti G: A phase-1 trial of bexarotene and denileukin diftitox in patients with relapsed or refractory cutaneous T-cell lymphoma. Blood. 2005 Jul 15;106(2):454-7. Epub 2005 Apr 5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15811959 +# Foss F: Clinical experience with denileukin diftitox (ONTAK). Semin Oncol. 2006 Feb;33(1 Suppl 3):S11-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16516670 +# Duvic M, Talpur R: Optimizing denileukin diftitox (Ontak) therapy. Future Oncol. 2008 Aug;4(4):457-69. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/18684057 +# Turturro F: Denileukin diftitox: a biotherapeutic paradigm shift in the treatment of lymphoid-derived disorders. Expert Rev Anticancer Ther. 2007 Jan;7(1):11-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17187516 +# Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11752352 + yes + + Interleukin-2 receptor subunit beta + Involved in hematopoietin/interferon-class (D200-domain) cytokine receptor activity + Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2 + IL2RB + 22q13|22q13.1 + Membrane; single-pass type I membrane protein + 241-265 + + 4.68 + 61118.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:6009 + + + GenAtlas + IL2RB + + + GeneCards + IL2RB + + + GenBank Gene Database + M26062 + + + GenBank Protein Database + 307048 + + + UniProtKB + P14784 + + + UniProt Accession + IL2RB_HUMAN + + + + CD122 antigen + High affinity IL-2 receptor subunit beta + IL-2 receptor + Interleukin-2 receptor subunit beta precursor + P70-75 + p75 + + >Interleukin-2 receptor beta chain precursor +MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQ +VHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMA +IQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEE +APLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDT +IPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDV +QKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFT +NQGYFFFHLPDALEIEACQVYFTYDPYSEEDPDEGVAGAPTGSSPQPLQPLSGEDDAYCT +FPSRDDLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVP +DLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQ +ELQGQDPTHLV + >1656 bp +ATGGCGGCCCCTGCTCTGTCCTGGCGTCTGCCCCTCCTCATCCTCCTCCTGCCCCTGGCT +ACCTCTTGGGCATCTGCAGCGGTGAATGGCACTTCCCAGTTCACATGCTTCTACAACTCG +AGAGCCAACATCTCCTGTGTCTGGAGCCAAGATGGGGCTCTGCAGGACACTTCCTGCCAA +GTCCATGCCTGGCCGGACAGACGGCGGTGGAACCAAACCTGTGAGCTGCTCCCCGTGAGT +CAAGCATCCTGGGCCTGCAACCTGATCCTCGGAGCCCCAGATTCTCAGAAACTGACCACA +GTTGACATCGTCACCCTGAGGGTGCTGTGCCGTGAGGGGGTGCGATGGAGGGTGATGGCC +ATCCAGGACTTCAAGCCCTTTGAGAACCTTCGCCTGATGGCCCCCATCTCCCTCCAAGTT +GTCCACGTGGAGACCCACAGATGCAACATAAGCTGGGAAATCTCCCAAGCCTCCCACTAC +TTTGAAAGACACCTGGAGTTCGAGGCCCGGACGCTGTCCCCAGGCCACACCTGGGAGGAG +GCCCCCCTGCTGACTCTCAAGCAGAAGCAGGAATGGATCTGCCTGGAGACGCTCACCCCA +GACACCCAGTATGAGTTTCAGGTGCGGGTCAAGCCTCTGCAAGGCGAGTTCACGACCTGG +AGCCCCTGGAGCCAGCCCCTGGCCTTCAGGACAAAGCCTGCAGCCCTTGGGAAGGACACC +ATTCCGTGGCTCGGCCACCTCCTCGTGGGCCTCAGCGGGGCTTTTGGCTTCATCATCTTA +GTGTACTTGCTGATCAACTGCAGGAACACCGGGCCATGGCTGAAGAAGGTCCTGAAGTGT +AACACCCCAGACCCCTCGAAGTTCTTTTCCCAGCTGAGCTCAGAGCATGGAGGAGACGTC +CAGAAGTGGCTCTCTTCGCCCTTCCCCTCATCGTCCTTCAGCCCTGGCGGCCTGGCACCT +GAGATCTCGCCACTAGAAGTGCTGGAGAGGGACAAGGTGACGCAGCTGCTCCTGCAGCAG +GACAAGGTGCCTGAGCCCGCATCCTTAAGCAGCAACCACTCGCTGACCAGCTGCTTCACC +AACCAGGGTTACTTCTTCTTCCACCTCCCGGATGCCTTGGAGATAGAGGCCTGCCAGGTG +TACTTTACTTACGACCCCTACTCAGAGGAAGACCCTGATGAGGGTGTGGCCGGGGCACCC +ACAGGGTCTTCCCCCCAACCCCTGCAGCCTCTGTCAGGGGAGGACGACGCCTACTGCACC +TTCCCCTCCAGGGATGACCTGCTGCTCTTCTCCCCCAGTCTCCTCGGTGGCCCCAGCCCC +CCAAGCACTGCCCCTGGGGGCAGTGGGGCCGGTGAAGAGAGGATGCCCCCTTCTTTGCAA +GAAAGAGTCCCCAGAGACTGGGACCCCCAGCCCCTGGGGCCTCCCACCCCAGGAGTCCCA +GACCTGGTGGATTTTCAGCCACCCCCTGAGCTGGTGCTGCGAGAGGCTGGGGAGGAGGTC +CCTGACGCTGGCCCCAGGGAGGGAGTCAGTTTCCCCTGGTCCAGGCCTCCTGGGCAGGGG +GAGTTCAGGGCCCTTAATGCTCGCCTGCCCCTGAACACTGATGCCTACTTGTCCCTCCAA +GAACTCCAGGGTCAGGACCCAACTCACTTGGTGTAG + + + + + component + cell + + + component + membrane + + + function + signal transducer activity + + + function + receptor activity + + + function + transmembrane receptor activity + + + function + hematopoietin/interferon-class (D200-domain) cytokine receptor activity + + + + + + BE0002102 + Cytokine receptor common subunit gamma + Human + + # Foss F, Demierre MF, DiVenuti G: A phase-1 trial of bexarotene and denileukin diftitox in patients with relapsed or refractory cutaneous T-cell lymphoma. Blood. 2005 Jul 15;106(2):454-7. Epub 2005 Apr 5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15811959 +# Foss F: Clinical experience with denileukin diftitox (ONTAK). Semin Oncol. 2006 Feb;33(1 Suppl 3):S11-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16516670 +# Foss FM: DAB(389)IL-2 (denileukin diftitox, ONTAK): a new fusion protein technology. Clin Lymphoma. 2000 Nov;1 Suppl 1:S27-31. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11707860 + unknown + + Cytokine receptor common subunit gamma + + Common subunit for the receptors for a variety of interleukins + IL2RG + Xq13.1 + Membrane + 263-283 + + 6.31 + 42287.0 + + Human + + + HUGO Gene Nomenclature Committee (HGNC) + HGNC:6010 + + + GenAtlas + IL2RG + + + GeneCards + IL2RG + + + GenBank Gene Database + D11086 + + + GenBank Protein Database + 219890 + + + UniProtKB + P31785 + + + UniProt Accession + IL2RG_HUMAN + + + + CD132 antigen + Cytokine receptor common gamma chain precursor + Gamma-C + IL-2R gamma chain + Interleukin- 2 receptor gamma chain + p64 + + >Cytokine receptor common gamma chain +MLKPSLPFTSLLFLQLPLLGVGLNTTILTPNGNEDTTADFFLTTMPTDSLSVSTLPLPEV +QCFVFNVEYMNCTWNSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKK +EIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLN +HCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEW +SHPIHWGSNTSKENPFLFALEAVVISVGSMGLIISLLCVYFWLERTMPRIPTLKNLEDLV +TEYHGNFSAWSGVSKGLAESLQPDYSERLCLVSEIPPKGGALGEGPGASPCNQHSPYWAP +PCYTLKPET + >1110 bp +ATGTTGAAGCCATCATTACCATTCACATCCCTCTTATTCCTGCAGCTGCCCCTGCTGGGA +GTGGGGCTGAACACGACAATTCTGACGCCCAATGGGAATGAAGACACCACAGCTGATTTC +TTCCTGACCACTATGCCCACTGACTCCCTCAGTGTTTCCACTCTGCCCCTCCCAGAGGTT +CAGTGTTTTGTGTTCAATGTCGAGTACATGAATTGCACTTGGAACAGCAGCTCTGAGCCC +CAGCCTACCAACCTCACTCTGCATTATTGGTACAAGAACTCGGATAATGATAAAGTCCAG +AAGTGCAGCCACTATCTATTCTCTGAAGAAATCACTTCTGGCTGTCAGTTGCAAAAAAAG +GAGATCCACCTCTACCAAACATTTGTTGTTCAGCTCCAGGACCCACGGGAACCCAGGAGA +CAGGCCACACAGATGCTAAAACTGCAGAATCTGGTGATCCCCTGGGCTCCAGAGAACCTA +ACACTTCACAAACTGAGTGAATCCCAGCTAGAACTGAACTGGAACAACAGATTCTTGAAC +CACTGTTTGGAGCACTTGGTGCAGTACCGGACTGACTGGGACCACAGCTGGACTGAACAA +TCAGTGGATTATAGACATAAGTTCTCCTTGCCTAGTGTGGATGGGCAGAAACGCTACACG +TTTCGTGTTCGGAGCCGCTTTAACCCACTCTGTGGAAGTGCTCAGCATTGGAGTGAATGG +AGCCACCCAATCCACTGGGGGAGCAATACTTCAAAAGAGAATCCTTTCCTGTTTGCATTG +GAAGCCGTGGTTATCTCTGTTGGCTCCATGGGATTGATTATCAGCCTTCTCTGTGTGTAT +TTCTGGCTGGAACGGACGATGCCCCGAATTCCCACCCTGAAGAACCTAGAGGATCTTGTT +ACTGAATACCACGGGAACTTTTCGGCCTGGAGTGGTGTGTCTAAGGGACTGGCTGAGAGT +CTGCAGCCAGACTACAGTGAACGACTCTGCCTCGTCAGTGAGATTCCCCCAAAAGGAGGG +GCCCTTGGGGAGGGGCCTGGGGCCTCCCCATGCAACCAGCATAGCCCCTACTGGGCCCCC +CCATGTTACACCCTAAAGCCTGAAACCTGA + + + + + component + cell + + + component + membrane + + + function + signal transducer activity + + + function + receptor activity + + + function + transmembrane receptor activity + + + function + hematopoietin/interferon-class (D200-domain) cytokine receptor activity + + + + + + + + +
+ diff --git a/src/msk/drugbank4/DrugBankParser.java b/src/msk/drugbank4/DrugBankParser.java index 25f12cf..8b8b457 100644 --- a/src/msk/drugbank4/DrugBankParser.java +++ b/src/msk/drugbank4/DrugBankParser.java @@ -21,11 +21,11 @@ import java.util.List; import java.util.Set; -import org.jdom.Document; -import org.jdom.Element; -import org.jdom.JDOMException; -import org.jdom.Namespace; -import org.jdom.input.SAXBuilder; +import org.jdom2.Document; +import org.jdom2.Element; +import org.jdom2.JDOMException; +import org.jdom2.Namespace; +import org.jdom2.input.SAXBuilder; /** * Download XML file from Drugbank (http://www.drugbank.ca/downloads) diff --git a/test/msk/drugbank4/test/Test.java b/test/msk/drugbank4/test/Test.java new file mode 100644 index 0000000..5cad549 --- /dev/null +++ b/test/msk/drugbank4/test/Test.java @@ -0,0 +1,42 @@ +package msk.drugbank4.test; + +import java.io.File; +import java.io.IOException; +import java.util.Set; + +import msk.drugbank4.DrugBankParser; +import msk.drugbank4.DrugModel; + +import org.jdom2.JDOMException; +import org.junit.Assert; +import org.junit.Before; + +public class Test { + + private File drugbankXmlFile; + @Before + public void setUp() throws Exception { + drugbankXmlFile = new File("resources/drugbank-example.xml"); + } + + @org.junit.Test + public void test() { + DrugBankParser parser = new DrugBankParser(); + try { + Set drugs = parser.parse(drugbankXmlFile); + Assert.assertTrue(drugs.size() == 4); + for(DrugModel d : drugs) { + if(d.getName().equals("Cetuximab")) { + Assert.assertTrue(d.getTargets().size() == 12); + } + } + } catch (JDOMException e) { + // TODO Auto-generated catch block + e.printStackTrace(); + } catch (IOException e) { + // TODO Auto-generated catch block + e.printStackTrace(); + } + } + +}