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 Berlex Labs 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 >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 DB01022 Phylloquinone 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 binding function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis 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/m² 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 02271249 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 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 function nucleotide binding function ATP binding 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 calcium ion binding function binding function peptidase activity function endopeptidase activity function catalytic activity function serine-type endopeptidase activity function hydrolase activity function ion binding function cation binding 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 process response to biotic stimulus process defense response process protein metabolism process immune response 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic anion 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic anion 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic 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 calcium ion binding function binding function peptidase activity function endopeptidase activity function catalytic activity function serine-type endopeptidase activity function hydrolase activity function ion binding function cation binding 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 process response to biotic stimulus process defense response process protein metabolism process immune response 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 Roche (Chile) 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 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 >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 DB00005 BIOD00052 BTD00052 Etanercept Dimeric fusion protein consisting of the extracellular ligand-binding portion of the human 75 kilodalton (p75) tumor necrosis factor receptor (TNFR) linked to the Fc portion of human IgG1. The Fc component of etanercept contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. Etanercept is produced by recombinant DNA technology in a Chinese hamster ovary (CHO) mammalian cell expression system. It consists of 934 amino acids 185243-69-0 approved investigational # http://www.genome.jp/dbget-bin/www_bget?D00742 #American Society of Health System Pharmacists, Inc., DynaMed [Internet]. Ipswich (MA): EBSCO Information Services. 1995. Etanercept; [updated 2014 Sept 24 cited 2014 Nov 11]. Available from http://web.b.ebscohost.com.login.ezproxy.library.ualberta.ca/dynamed/detail?vid=4&sid=eeea413d-1490-4efa-bf5d-71f40e1986a1%40sessionmgr111&hid=123&bdata=JnNpdGU9ZHluYW1lZC1saXZlJnNjb3BlPXNpdGU%3d#db=dme&AN=232781 Timothy D. Osslund, Christi L. Clogston, Shon Lee Crampton, Randal B. Bass, "Crystals of etanercept and methods of making thereof." U.S. Patent US07276477, issued October 02, 2007. For treatment of severe active rheumatoid arthritis in adults, severe juvenile idiopathic arthritis, ankylosing spondylitis, and severe plaque psoriasis. Tumor necrosis factor TNF is a naturally occurring cytokine that is involved in normal inflammatory and immune responses. Elevated levels of TNF are found in tissues and fluids of patients with rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis (AS), and plaque psoriasis. Etanercept binds specifically to tumor necrosis factor (TNF) and blocks its interaction with cell surface TNF receptors. There are two distinct receptors for TNF (TNFRs), a 55 kilodalton protein (p55) and a 75 kilodalton protein (p75). The biological activity of TNF is dependent upon binding to either cell surface receptor (p75 or p55). Etanercept is a dimeric soluble form of the p75 TNF receptor that can bind to two TNF molecules, thereby effectively removing them from circulation. Bioavailability following sub-Q administration is approximately 60%. Peak plasma concentrations achieved within 69 hours. 102 +/- 30 hrs in individuals with rheumatoid arthritis and 68 hours in healthy adults * 160 +/- 80 mL/hr [RA patients] Peptides Organic Compounds Organic Acids Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues CD120b p75 p80 TNF-alpha receptor TNF-R2 Tumor necrosis factor receptor 2 Tumor necrosis factor receptor superfamily member 1B precursor Tumor necrosis factor receptor type II Enbrel 58406-425_491e2358-832f-46a6-aae4-0bc35490ff48 58406-425 2003-01-02 kit BLA103795 false false true US FDA NDC Enbrel 58406-435_491e2358-832f-46a6-aae4-0bc35490ff48 58406-435 2005-10-06 solution 50 mg/mL subcutaneous BLA103795 false false true US FDA NDC Enbrel 58406-445_491e2358-832f-46a6-aae4-0bc35490ff48 58406-445 2005-11-10 solution 50 mg/mL subcutaneous BLA103795 false false true US FDA NDC Enbrel 58406-455_491e2358-832f-46a6-aae4-0bc35490ff48 58406-455 2005-11-10 solution 25 mg/.5mL subcutaneous BLA103795 false false true US FDA NDC Enbrel 02274728 solution 50 mg subcutaneous false false true Canada DPD Enbrel Sureclick Amgen Inc. http://www.amgen.com Boehringer Ingelheim Ltd. http://www.boehringer-ingelheim.com DSM Corp. http://www.dsm.com Immunex Corp. Physicians Total Care Inc. http://www.physicianstotalcare.com Vetter Pharma Fertigung GmbH and Co. KG http://www.vetter-pharma.com Amgen Inc. + Wyeth + Takeda Enbrel 25 mg kit 250.37 each Enbrel 50 mg/ml sureclick syr 488.74 syringe Enbrel 4 25 mg Kit (1 Box = 1 Kit = Four 25 mg Vials) 1016.57 box Enbrel (1 Box = 1 Kit = Four 50 mg Syringes) 3.92ml Box 2033.14 box Enbrel SureClick (1 Box Contains Four 50 mg Prefilled Autoinjectors) 2033.14 box Immunosuppressive Agents Humans and other mammals

Kit

Solution

subcutaneous 25 mg/.5mL

Solution

subcutaneous 50 mg

Solution

subcutaneous 50 mg/mL ANTINEOPLASTIC AND IMMUNOMODULATING AGENTS IMMUNOSUPPRESSANTS IMMUNOSUPPRESSANTS Tumor necrosis factor alpha (TNF-α) inhibitors 92:00.00 2123593 Canada 2000-03-14 2013-09-14 2476934 Canada 2009-06-16 2023-02-27 36755 United States 2000-06-27 2012-10-23 7276477 United States 2007-10-02 2024-07-29 DB01281 Abatacept Anti-TNF Agents may enhance the adverse/toxic effect of Abatacept. An increased risk of serious infection during concomitant use has been reported. DB00026 Anakinra Anti-TNF Agents may enhance the adverse/toxic effect of Anakinra. An increased risk of serious infection during concomitant use has been reported. DB08879 Belimumab Etanercept may enhance the adverse/toxic effect of Belimumab. DB06168 Canakinumab Anti-TNF Agents may enhance the adverse/toxic effect of Canakinumab. Specifically, the risk for serious infections and/or neutropenia may be increased. DB08904 Certolizumab pegol Anti-TNF Agents may enhance the immunosuppressive effect of Certolizumab Pegol. DB00531 Cyclophosphamide Etanercept may enhance the adverse/toxic effect of Cyclophosphamide. An increased risk of solid cancer development may be present. DB06643 Denosumab May enhance the adverse/toxic effect of Immunosuppressants. Specifically, the risk for serious infections may be increased. DB00065 Infliximab Etanercept may enhance the immunosuppressive effect of InFLIXimab. DB01097 Leflunomide Immunosuppressants may enhance the adverse/toxic effect of Leflunomide. Specifically, the risk for hematologic toxicity such as pancytopenia, agranulocytosis, and/or thrombocytopenia may be increased. DB00108 Natalizumab Immunosuppressants may enhance the adverse/toxic effect of Natalizumab. Specifically, the risk of concurrent infection may be increased. DB00337 Pimecrolimus May enhance the adverse/toxic effect of Immunosuppressants. DB06372 Rilonacept Anti-TNF Agents may enhance the adverse/toxic effect of Rilonacept. DB01656 Roflumilast May enhance the immunosuppressive effect of Immunosuppressants. DB06688 Sipuleucel-T Immunosuppressants may diminish the therapeutic effect of Sipuleucel-T. DB06273 Tocilizumab May enhance the immunosuppressive effect of Anti-TNF Agents. DB08895 Tofacitinib Anti-TNF Agents may enhance the adverse/toxic effect of Tofacitinib. DB00072 Trastuzumab May enhance the neutropenic effect of Immunosuppressants. DB09033 Vedolizumab Anti-TNF Agents may enhance the adverse/toxic effect of Vedolizumab. > Etanercept Sequence LPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPGQHAKVFCTKTSDTVCDSCEDST YTQLWNWVPECLSCGSRCSSDQVETQACTREQNRICTCRPGWYCALSKQEGCRLCAPLRK CRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICRPHQICNVVAIPGNASMDAVCTS TSPTRSMAPGAVHLPQPVSTRSQHTQPTPEPSTAPSTSFLLPMGPSPPAEGSTGDEPKSC DKTHTCPPCPAPELLGGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVD GVEVHNAKTKPREEQYNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAK GQPREPQVYTLPPSREEMTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDS DGSFFLYSKLTVDKSRWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK Melting Point 71 °C (whole mAb) Vermeer, A.W.P. & Norde, W., Biophys. J. 78:394-404 (2000) Hydrophobicity -0.529 Isoelectric Point 7.89 Molecular Weight 51234.9000 Molecular Formula C2224H3475N621O698S36 KEGG Compound C07897 KEGG Drug D00742 National Drug Code Directory 58406-455-04 GenBank M32315 PharmGKB PA449515 UniProtKB P20333 Wikipedia Etanercept RxList http://www.rxlist.com/cgi/generic/etanercept.htm Drugs.com http://www.drugs.com/cdi/etanercept.html BE0000704 Tumor necrosis factor Human antibody # Park YC, Burkitt V, Villa AR, Tong L, Wu H: Structural basis for self-association and receptor recognition of human TRAF2. Nature. 1999 Apr 8;398(6727):533-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10206649 # Sandborn WJ, Hanauer SB: Antitumor necrosis factor therapy for inflammatory bowel disease: a review of agents, pharmacology, clinical results, and safety. Inflamm Bowel Dis. 1999 May;5(2):119-33. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10338381 # Grell M, Zimmermann G, Gottfried E, Chen CM, Grunwald U, Huang DC, Wu Lee YH, Durkop H, Engelmann H, Scheurich P, Wajant H, Strasser A: Induction of cell death by tumour necrosis factor (TNF) receptor 2, CD40 and CD30: a role for TNF-R1 activation by endogenous membrane-anchored TNF. EMBO J. 1999 Jun 1;18(11):3034-43. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10357816 # Moreland LW: Inhibitors of tumor necrosis factor: new treatment options for rheumatoid arthritis. Cleve Clin J Med. 1999 Jun;66(6):367-74. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10375846 # Calabrese LH: Rheumatoid arthritis and primary care: the case for early diagnosis and treatment. J Am Osteopath Assoc. 1999 Jun;99(6):313-21. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10405518 # 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 Tumor necrosis factor Involved in tumor necrosis factor receptor binding Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin 1 secretion and is implicated in the induction of cachexia, Under certain conditions it can stimulate cell proliferation and induce cell differentiation TNF 6p21.3 Cell membrane; single-pass type II membrane protein. Processed form:Secreted protein. Also exists as 36-56 6.92 25645.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:11892 GenAtlas TNF GeneCards TNF GenBank Gene Database M16441 GenBank Protein Database 339741 UniProtKB P01375 UniProt Accession TNFA_HUMAN Cachectin TNF-a TNF-alpha Tumor necrosis factor ligand superfamily member 2 Tumor necrosis factor precursor >Tumor necrosis factor precursor MSTESMIRDVELAEEALPKKTGGPQGSRRCLFLSLFSFLIVAGATTLFCLLHFGVIGPQR EEFPRDLSLISPLAQAVRSSSRTPSDKPVAHVVANPQAEGQLQWLNRRANALLANGVELR DNQLVVPSEGLYLIYSQVLFKGQGCPSTHVLLTHTISRIAVSYQTKVNLLSAIKSPCQRE TPEGAEAKPWYEPIYLGGVFQLEKGDRLSAEINRPDYLDFAESGQVYFGIIAL >702 bp ATGAGCACTGAAAGCATGATCCGGGACGTGGAGCTGGCCGAGGAGGCGCTCCCCAAGAAG ACAGGGGGGCCCCAGGGCTCCAGGCGGTGCTTGTTCCTCAGCCTCTTCTCCTTCCTGATC GTGGCAGGCGCCACCACGCTCTTCTGCCTGCTGCACTTTGGAGTGATCGGCCCCCAGAGG GAAGAGTTCCCCAGGGACCTCTCTCTAATCAGCCCTCTGGCCCAGGCAGTCAGATCATCT TCTCGAACCCCGAGTGACAAGCCTGTAGCCCATGTTGTAGCAAACCCTCAAGCTGAGGGG CAGCTCCAGTGGCTGAACCGCCGGGCCAATGCCCTCCTGGCCAATGGCGTGGAGCTGAGA GATAACCAGCTGGTGGTGCCATCAGAGGGCCTGTACCTCATCTACTCCCAGGTCCTCTTC AAGGGCCAAGGCTGCCCCTCCACCCATGTGCTCCTCACCCACACCATCAGCCGCATCGCC GTCTCCTACCAGACCAAGGTCAACCTCCTCTCTGCCATCAAGAGCCCCTGCCAGAGGGAG ACCCCAGAGGGGGCTGAGGCCAAGCCCTGGTATGAGCCCATCTATCTGGGAGGGGTCTTC CAGCTGGAGAAGGGTGACCGACTCAGCGCTGAGATCAATCGGCCCGACTATCTCGACTTT GCCGAGTCTGGGCAGGTCTACTTTGGGATCATTGCCCTGTGA PF00229 TNF component cell component membrane function tumor necrosis factor receptor binding function signal transducer activity function receptor binding function cytokine activity process response to stimulus process response to biotic stimulus process defense response process immune response BE0000949 Tumor necrosis factor receptor superfamily member 1B Human # 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 unknown Tumor necrosis factor receptor superfamily member 1B Involved in tumor necrosis factor receptor activity Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2. This receptor mediates most of the metabolic effects of TNF-alpha. Isoform 2 blocks TNF-alpha-induced apoptosis, which suggests that it regulates TNF-alpha function by antagonizing its biological activity TNFRSF1B 1p36.3-p36.2 Isoform 1:Cell membrane; single-pass type I membrane protein. Isoform 2:Secreted protein. TBP-II:Sec 258-287 6.22 48291.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:11917 GenAtlas TNFRSF1B GeneCards TNFRSF1B GenBank Gene Database M32315 GenBank Protein Database 189186 UniProtKB P20333 UniProt Accession TNR1B_HUMAN CD120b antigen Etanercept p75 p80 TNF-alpha receptor TNF-R2 Tumor necrosis factor receptor 2 Tumor necrosis factor receptor superfamily member 1B precursor Tumor necrosis factor receptor type II >Tumor necrosis factor receptor superfamily member 1B precursor MAPVAVWAALAVGLELWAAAHALPAQVAFTPYAPEPGSTCRLREYYDQTAQMCCSKCSPG QHAKVFCTKTSDTVCDSCEDSTYTQLWNWVPECLSCGSRCSSDQVETQACTREQNRICTC RPGWYCALSKQEGCRLCAPLRKCRPGFGVARPGTETSDVVCKPCAPGTFSNTTSSTDICR PHQICNVVAIPGNASMDAVCTSTSPTRSMAPGAVHLPQPVSTRSQHTQPTPEPSTAPSTS FLLPMGPSPPAEGSTGDFALPVGLIVGVTALGLLIIGVVNCVIMTQVKKKPLCLQREAKV PHLPADKARGTQGPEQQHLLITAPSSSSSSLESSASALDRRAPTRNQPQAPGVEASGAGE ARASTGSSDSSPGGHGTQVNVTCIVNVCSSSDHSSQCSSQASSTMGDTDSSPSESPKDEQ VPFSKEECAFRSQLETPETLLGSTEEKPLPLGVPDAGMKPS >1386 bp ATGGCGCCCGTCGCCGTCTGGGCCGCGCTGGCCGTCGGACTGGAGCTCTGGGCTGCGGCG CACGCCTTGCCCGCCCAGGTGGCATTTACACCCTACGCCCCGGAGCCCGGGAGCACATGC CGGCTCAGAGAATACTATGACCAGACAGCTCAGATGTGCTGCAGCAAATGCTCGCCGGGC CAACATGCAAAAGTCTTCTGTACCAAGACCTCGGACACCGTGTGTGACTCCTGTGAGGAC AGCACATACACCCAGCTCTGGAACTGGGTTCCCGAGTGCTTGAGCTGTGGCTCCCGCTGT AGCTCTGACCAGGTGGAAACTCAAGCCTGCACTCGGGAACAGAACCGCATCTGCACCTGC AGGCCCGGCTGGTACTGCGCGCTGAGCAAGCAGGAGGGGTGCCGGCTGTGCGCGCCGCTG CGCAAGTGCCGCCCGGGCTTCGGCGTGGCCAGACCAGGAACTGAAACATCAGACGTGGTG TGCAAGCCCTGTGCCCCGGGGACGTTCTCCAACACGACTTCATCCACGGATATTTGCAGG CCCCACCAGATCTGTAACGTGGTGGCCATCCCTGGGAATGCAAGCATGGATGCAGTCTGC ACGTCCACGTCCCCCACCCGGAGTATGGCCCCAGGGGCAGTACACTTACCCCAGCCAGTG TCCACACGATCCCAACACACGCAGCCAACTCCAGAACCCAGCACTGCTCCAAGCACCTCC TTCCTGCTCCCAATGGGCCCCAGCCCCCCAGCTGAAGGGAGCACTGGCGACTTCGCTCTT CCAGTTGGACTGATTGTGGGTGTGACAGCCTTGGGTCTACTAATAATAGGAGTGGTGAAC TGTGTCATCATGACCCAGGTGAAAAAGAAGCCCTTGTGCCTGCAGAGAGAAGCCAAGGTG CCTCACTTGCCTGCCGATAAGGCCCGGGGTACACAGGGCCCCGAGCAGCAGCACCTGCTG ATCACAGCGCCGAGCTCCAGCAGCAGCTCCCTGGAGAGCTCGGCCAGTGCGTTGGACAGA AGGGCGCCCACTCGGAACCAGCCACAGGCACCAGGCGTGGAGGCCAGTGGGGCCGGGGAG GCCCGGGCCAGCACCGGGAGCTCAGATTCTTCCCCTGGTGGCCATGGGACCCAGGTCAAT GTCACCTGCATCGTGAACGTCTGTAGCAGCTCTGACCACAGCTCACAGTGCTCCTCCCAA GCCAGCTCCACAATGGGAGACACAGATTCCAGCCCCTCGGAGTCCCCGAAGGACGAGCAG GTCCCCTTCTCCAAGGAGGAATGTGCCTTTCGGTCACAGCTGGAGACGCCAGAGACCCTG CTGGGGAGCACCGAAGAGAAGCCCCTGCCCCTTGGAGTGCCTGATGCTGGGATGAAGCCC AGTTAA PF00020 TNFR_c6 component cell component intrinsic to membrane component integral to membrane component membrane function death receptor activity function tumor necrosis factor receptor activity function signal transducer activity function receptor activity function transmembrane receptor activity process signal transduction process cell surface receptor linked signal transduction process cytokine and chemokine mediated signaling pathway process cellular process process cell communication BE0000710 High affinity immunoglobulin gamma Fc receptor I 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 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 BE0002097 Low affinity immunoglobulin gamma Fc region receptor III-A Human # Criswell LA, Lum RF, Turner KN, Woehl B, Zhu Y, Wang J, Tiwari HK, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL Jr: The influence of genetic variation in the HLA-DRB1 and LTA-TNF regions on the response to treatment of early rheumatoid arthritis with methotrexate or etanercept. Arthritis Rheum. 2004 Sep;50(9):2750-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15457442 # Hughes LB, Criswell LA, Beasley TM, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL: Genetic risk factors for infection in patients with early rheumatoid arthritis. Genes Immun. 2004 Dec;5(8):641-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15526004 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 BE0002098 Low affinity immunoglobulin gamma Fc region receptor II-a Human # Criswell LA, Lum RF, Turner KN, Woehl B, Zhu Y, Wang J, Tiwari HK, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL Jr: The influence of genetic variation in the HLA-DRB1 and LTA-TNF regions on the response to treatment of early rheumatoid arthritis with methotrexate or etanercept. Arthritis Rheum. 2004 Sep;50(9):2750-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15457442 # Hughes LB, Criswell LA, Beasley TM, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL: Genetic risk factors for infection in patients with early rheumatoid arthritis. Genes Immun. 2004 Dec;5(8):641-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15526004 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 # Hart SP, Ross JA, Ross K, Haslett C, Dransfield I: Molecular characterization of the surface of apoptotic neutrophils: implications for functional downregulation and recognition by phagocytes. Cell Death Differ. 2000 May;7(5):493-503. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10800083 # Ranheim EA, Kipps TJ: Tumor necrosis factor-alpha facilitates induction of CD80 (B7-1) and CD54 on human B cells by activated T cells: complex regulation by IL-4, IL-10, and CD40L. Cell Immunol. 1995 Apr 1;161(2):226-35. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/7535196 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 BE0001087 Lymphotoxin-alpha Human # Johnson CJ, Reilly KM, Murray KM: Etanercept in juvenile rheumatoid arthritis. Ann Pharmacother. 2001 Apr;35(4):464-71. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11302411 # Pennica D, Lam VT, Mize NK, Weber RF, Lewis M, Fendly BM, Lipari MT, Goeddel DV: Biochemical properties of the 75-kDa tumor necrosis factor receptor. Characterization of ligand binding, internalization, and receptor phosphorylation. J Biol Chem. 1992 Oct 15;267(29):21172-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/1328224 # Gudbrandsdottir S, Larsen R, Sorensen LK, Nielsen S, Hansen MB, Svenson M, Bendtzen K, Muller K: TNF and LT binding capacities in the plasma of arthritis patients: effect of etanercept treatment in juvenile idiopathic arthritis. Clin Exp Rheumatol. 2004 Jan-Feb;22(1):118-24. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15005015 # Buch MH, Conaghan PG, Quinn MA, Bingham SJ, Veale D, Emery P: True infliximab resistance in rheumatoid arthritis: a role for lymphotoxin alpha? Ann Rheum Dis. 2004 Oct;63(10):1344-6. Epub 2004 Mar 19. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15033655 # Kang CP, Lee KW, Yoo DH, Kang C, Bae SC: The influence of a polymorphism at position -857 of the tumour necrosis factor alpha gene on clinical response to etanercept therapy in rheumatoid arthritis. Rheumatology (Oxford). 2005 Apr;44(4):547-52. Epub 2005 Feb 3. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15695296 unknown Lymphotoxin-alpha Involved in tumor necrosis factor receptor binding Cytokine that in its homotrimeric form binds to TNFRSF1A/TNFR1, TNFRSF1B/TNFBR and TNFRSF14/HVEM. In its heterotrimeric form with LTB binds to TNFRSF3/LTBR. Lymphotoxin is produced by lymphocytes and cytotoxic for a wide range of tumor cells in vitro and in vivo LTA 6p21.3 Homotrimer:Secreted protein. Heterotrimer:Membrane None 9.36 22297.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:6709 GenAtlas LTA GeneCards LTA GenBank Gene Database X01393 GenBank Protein Database 34445 UniProtKB P01374 UniProt Accession TNFB_HUMAN LT-alpha Lymphotoxin-alpha precursor TNF-beta Tumor necrosis factor ligand superfamily member 1 >Lymphotoxin-alpha precursor MTPPERLFLPRVCGTTLHLLLLGLLLVLLPGAQGLPGVGLTPSAAQTARQHPKMHLAHST LKPAAHLIGDPSKQNSLLWRANTDRAFLQDGFSLSNNSLLVPTSGIYFVYSQVVFSGKAY SPKATSSPLYLAHEVQLFSSQYPFHVPLLSSQKMVYPGLQEPWLHSMYHGAAFQLTQGDQ LSTHTDGIPHLVLSPSTVFFGAFAL >618 bp ATGACACCACCTGAACGTCTCTTCCTCCCAAGGGTGTGTGGCACCACCCTACACCTCCTC CTTCTGGGGCTGCTGCTGGTTCTGCTGCCTGGGGCCCAGGGGCTCCCTGGTGTTGGCCTC ACACCTTCAGCTGCCCAGACTGCCCGTCAGCACCCCAAGATGCATCTTGCCCACAGCACC CTCAAACCTGCTGCTCACCTCATTGGAGACCCCAGCAAGCAGAACTCACTGCTCTGGAGA GCAAACACGGACCGTGCCTTCCTCCAGGATGGTTTCTCCTTGAGCAACAATTCTCTCCTG GTCCCCACCAGTGGCATCTACTTCGTCTACTCCCAGGTGGTCTTCTCTGGGAAAGCCTAC TCTCCCAAGGCCACCTCCTCCCCACTCTACCTGGCCCATGAGGTCCAGCTCTTCTCCTCC CAGTACCCCTTCCATGTGCCTCTCCTCAGCTCCCAGAAGATGGTGTATCCAGGGCTGCAG GAACCCTGGCTGCACTCGATGTACCACGGGGCTGCGTTCCAGCTCACCCAGGGAGACCAG CTATCCACCCACACAGATGGCATCCCCCACCTAGTCCTCAGCCCTAGTACTGTCTTCTTT GGAGCCTTCGCTCTGTAG PF00229 TNF component cell component membrane function tumor necrosis factor receptor binding function signal transducer activity function receptor binding function cytokine activity process response to stimulus process response to biotic stimulus process defense response process immune response BE0000901 Low affinity immunoglobulin gamma Fc region receptor III-B Human # Hart SP, Ross JA, Ross K, Haslett C, Dransfield I: Molecular characterization of the surface of apoptotic neutrophils: implications for functional downregulation and recognition by phagocytes. Cell Death Differ. 2000 May;7(5):493-503. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10800083 # Ozgocmen S, Godekmerdan A, Ozkurt-Zengin F: Acute-phase response, clinical measures and disease activity in ankylosing spondylitis. Joint Bone Spine. 2007 May;74(3):249-53. Epub 2007 Mar 5. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17387033 # Criswell LA, Lum RF, Turner KN, Woehl B, Zhu Y, Wang J, Tiwari HK, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL Jr: The influence of genetic variation in the HLA-DRB1 and LTA-TNF regions on the response to treatment of early rheumatoid arthritis with methotrexate or etanercept. Arthritis Rheum. 2004 Sep;50(9):2750-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15457442 # Hughes LB, Criswell LA, Beasley TM, Edberg JC, Kimberly RP, Moreland LW, Seldin MF, Bridges SL: Genetic risk factors for infection in patients with early rheumatoid arthritis. Genes Immun. 2004 Dec;5(8):641-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15526004 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 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 calcium ion binding function binding function peptidase activity function endopeptidase activity function catalytic activity function serine-type endopeptidase activity function hydrolase activity function ion binding function cation binding 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 process response to biotic stimulus process defense response process protein metabolism process immune response 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 calcium ion binding function binding function peptidase activity function endopeptidase activity function catalytic activity function serine-type endopeptidase activity function hydrolase activity function ion binding function cation binding 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 process response to biotic stimulus process defense response process protein metabolism process immune response 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic anion 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic anion 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 phosphate transport process physiological process process cellular physiological process process transport process ion transport process anion transport process inorganic anion transport BE0000262 Prostaglandin G/H synthase 2 Human inhibitor # Bawolak MT, Touzin K, Moreau ME, Desormeaux A, Adam A, Marceau F: Cardiovascular expression of inflammatory signaling molecules, the kinin B1 receptor and COX2, in the rabbit: effects of LPS, anti-inflammatory and anti-hypertensive drugs. Regul Pept. 2008 Feb 7;146(1-3):157-68. Epub 2007 Sep 14. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17931716 # Genovese T, Mazzon E, Crisafulli C, Di Paola R, Muia C, Bramanti P, Cuzzocrea S: Immunomodulatory effects of etanercept in an experimental model of spinal cord injury. J Pharmacol Exp Ther. 2006 Mar;316(3):1006-16. Epub 2005 Nov 22. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16303916 unknown Prostaglandin G/H synthase 2 Involved in peroxidase activity May have a role as a major mediator of inflammation and/or a role for prostanoid signaling in activity-dependent plasticity PTGS2 1q25.2-q25.3 Microsome; microsomal membrane; peripheral membrane protein None 7.41 68997.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:9605 GenAtlas PTGS2 GeneCards PTGS2 GenBank Gene Database L15326 GenBank Protein Database 291988 UniProtKB P35354 UniProt Accession PGH2_HUMAN COX-2 Cyclooxygenase- 2 EC 1.14.99.1 PGH synthase 2 PGHS-2 PHS II Prostaglandin G/H synthase 2 precursor Prostaglandin H2 synthase 2 Prostaglandin-endoperoxide synthase 2 >Prostaglandin G/H synthase 2 precursor MLARALLLCAVLALSHTANPCCSHPCQNRGVCMSVGFDQYKCDCTRTGFYGENCSTPEFL TRIKLFLKPTPNTVHYILTHFKGFWNVVNNIPFLRNAIMSYVLTSRSHLIDSPPTYNADY GYKSWEAFSNLSYYTRALPPVPDDCPTPLGVKGKKQLPDSNEIVEKLLLRRKFIPDPQGS NMMFAFFAQHFTHQFFKTDHKRGPAFTNGLGHGVDLNHIYGETLARQRKLRLFKDGKMKY QIIDGEMYPPTVKDTQAEMIYPPQVPEHLRFAVGQEVFGLVPGLMMYATIWLREHNRVCD VLKQEHPEWGDEQLFQTSRLILIGETIKIVIEDYVQHLSGYHFKLKFDPELLFNKQFQYQ NRIAAEFNTLYHWHPLLPDTFQIHDQKYNYQQFIYNNSILLEHGITQFVESFTRQIAGRV AGGRNVPPAVQKVSQASIDQSRQMKYQSFNEYRKRFMLKPYESFEELTGEKEMSAELEAL YGDIDAVELYPALLVEKPRPDAIFGETMVEVGAPFSLKGLMGNVICSPAYWKPSTFGGEV GFQIINTASIQSLICNNVKGCPFTSFSVPDPELIKTVTINASSSRSGLDDINPTVLLKER STEL >1815 bp ATGCTCGCCCGCGCCCTGCTGCTGTGCGCGGTCCTGGCGCTCAGCCATACAGCAAATCCT TGCTGTTCCCACCCATGTCAAAACCGAGGTGTATGTATGAGTGTGGGATTTGACCAGTAT AAGTGCGATTGTACCCGGACAGGATTCTATGGAGAAAACTGCTCAACACCGGAATTTTTG ACAAGAATAAAATTATTTCTGAAACCCACTCCAAACACAGTGCACTACATACTTACCCAC TTCAAGGGATTTTGGAACGTTGTGAATAACATTCCCTTCCTTCGAAATGCAATTATGAGT TATGTGTTGACATCCAGATCACATTTGATTGACAGTCCACCAACTTACAATGCTGACTAT GGCTACAAAAGCTGGGAAGCCTTCTCTAACCTCTCCTATTATACTAGAGCCCTTCCTCCT GTGCCTGATGATTGCCCGACTCCCTTGGGTGTCAAAGGTAAAAAGCAGCTTCCTGATTCA AATGAGATTGTGGAAAAATTGCTTCTAAGAAGAAAGTTCATCCCTGATCCCCAGGGCTCA AACATGATGTTTGCATTCTTTGCCCAGCACTTCACGCATCAGTTTTTCAAGACAGATCAT AAGCGAGGGCCAGCTTTCACCAACGGGCTGGGCCATGGGGTGGACTTAAATCATATTTAC GGTGAAACTCTGGCTAGACAGCGTAAACTGCGCCTTTTCAAGGATGGAAAAATGAAATAT CAGATAATTGATGGAGAGATGTATCCTCCCACAGTCAAAGATACTCAGGCAGAGATGATC TACCCTCCTCAAGTCCCTGAGCATCTACGGTTTGCTGTGGGGCAGGAGGTCTTTGGTCTG GTGCCTGGTCTGATGATGTATGCCACAATCTGGCTGCGGGAACACAACAGAGTATGCGAT GTGCTTAAACAGGAGCATCCTGAATGGGGTGATGAGCAGTTGTTCCAGACAAGCAGGCTA ATACTGATAGGAGAGACTATTAAGATTGTGATTGAAGATTATGTGCAACACTTGAGTGGC TATCACTTCAAACTGAAATTTGACCCAGAACTACTTTTCAACAAACAATTCCAGTACCAA AATCGTATTGCTGCTGAATTTAACACCCTCTATCACTGGCATCCCCTTCTGCCTGACACC TTTCAAATTCATGACCAGAAATACAACTATCAACAGTTTATCTACAACAACTCTATATTG CTGGAACATGGAATTACCCAGTTTGTTGAATCATTCACCAGGCAAATTGCTGGCAGGGTT GCTGGTGGTAGGAATGTTCCACCCGCAGTACAGAAAGTATCACAGGCTTCCACTGACCAG AGCAGGCAGATGAAATACCAGTCTTTTAATGAGTACCGCAAACGCTTTATGCTGAAGCCC TATGAATCATTTGAAGAACTTACAGGAGAAAAGGAAATGTCTGCAGAGTTGGAAGCACTC TATGGTGACATCGATGCTGTGGAGCTGTATCCTGCCCTTCTGGTAGAAAAGCCTCGGCCA GATGCCATCTTTGGTGAAACCATGGTAGAAGTTGGAGCACCATTCTCCTTGAAAGGACTT ATGGGTAATGTTATATGTTCTCCTGCCTACTGGAAGCCAAGCACTTTTGGTGGAGAAGTG GGTTTTCAAATCATCAACACTGCCTCAATTCAGTCTCTCATCTGCAATAACGTGAAGGGC TGTCCCTTTACTTCATTCAGTGTTCCAGATCCAGAGCTCATTAAAACAGTCACCATCAAT GCAAGTTCTTCCCGCTCCGGACTAGATGATATCAATCCCACAGTACTACTAAAAGAACGT TCGACTGAACTGTAG PF03098 An_peroxidase PF00008 EGF function antioxidant activity function peroxidase activity unknown unknown DB00006 BIOD00076 BTD00076 Bivalirudin Bivalirudin is a synthetic 20 residue peptide (thrombin inhibitor) which reversibly inhibits thrombin. Once bound to the active site, thrombin cannot activate fibrinogen into fibrin, the crucial step in the formation of thrombus. It is administered intravenously. Because it can cause blood stagnation, it is important to monitor changes in hematocrit, activated partial thromboplastin time, international normalized ratio and blood pressure. 128270-60-0 approved investigational # Seybert AL, Coons JC, Zerumsky K: Treatment of heparin-induced thrombocytopenia: is there a role for bivalirudin? Pharmacotherapy. 2006 Feb;26(2):229-41. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16466327 # Dager WE, Dougherty JA, Nguyen PH, Militello MA, Smythe MA: Heparin-induced thrombocytopenia: treatment options and special considerations. Pharmacotherapy. 2007 Apr;27(4):564-87. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/17381384 # Dang CH, Durkalski VL, Nappi JM: Evaluation of treatment with direct thrombin inhibitors in patients with heparin-induced thrombocytopenia. Pharmacotherapy. 2006 Apr;26(4):461-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16553503 # Robson R: The use of bivalirudin in patients with renal impairment. J Invasive Cardiol. 2000 Dec;12 Suppl F:33F-6. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11156732 # Van De Car DA, Rao SV, Ohman EM: Bivalirudin: a review of the pharmacology and clinical application. Expert Rev Cardiovasc Ther. 2010 Dec;8(12):1673-81. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/21108549 # Shammas NW: Bivalirudin: pharmacology and clinical applications. Cardiovasc Drug Rev. 2005 Winter;23(4):345-60. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16614733 # Gleason TG, Chengelis CP, Jackson CB, Lindstrom P: A 24-hour continuous infusion study of bivalirudin in the rat. Int J Toxicol. 2003 May-Jun;22(3):195-206. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/12851152 Avi Tovi, Chaim Eidelman, Shimon Shushan, Alon Hagi, Alexander Ivchenko, Gabriel-Marcus Butilca, Leah Bar-Oz, Tehila Gadi, Gil Zaovi, "Process for production of Bivalirudin." U.S. Patent US20070093423, issued April 26, 2007. For treatment of heparin-induced thrombocytopenia and for the prevention of thrombosis. Bivalirudin is indicated for use in patients undergoing percutaneous coronary intervention (PCI), in patients at moderate to high risk acute coronary syndromes due to unstable angina or non-ST segment elevation in whom a PCI is planned. Bivalirudin directly and reversibly inhibits thrombin by specifically binding both to the catalytic site and to the anion-binding exosite of circulating and clot-bound thrombin. The action of bivalirudin is reversible because thrombin will slowly cleave the thrombin-bivalirudin bond which recovers the active site of thrombin. Inhibits the action of thrombin by binding both to its catalytic site and to its anion-binding exosite. Thrombin is a serine proteinase that plays a central role in the thrombotic process, acting to cleave fibrinogen into fibrin monomers and to activate Factor XIII to Factor XIIIa, allowing fibrin to develop a covalently cross-linked framework which stabilizes the thrombus; thrombin also activates Factors V and VIII, promoting further thrombin generation, and activates platelets, stimulating aggregation and granule release. Based on a study by Gleason et al., the no-observed-adverse-effect level (NOAEL) for bivalirudin, administered to rats via intravenous infusion over a 24-hour period, was 2000 mg/kg/24 h. 80% proteolytic cleavage Following intravenous administration, bivalirudin exhibits linear pharmacokinetics . The mean steady state concentration is 12.3 +/- 1.7mcg/mL after administration of an intravenous bolus of 1mg/kg followd by a 2.5mg/kg/hr intravenous infusion given over 4 hours. * Normal renal function: 25 min (in normal conditions) * Creatinine clearance 10-29mL/min: 57min * Dialysis-dependant patients: 3.5h Other than thrombin and red blood cells, bivalirudin does not bind to plasma proteins. Bivalirudin is cleared from plasma by a combination of renal mechanisms (20%) and proteolytic cleavage. 0.2L/kg * 3.4 mL/min/kg [Normal renal function] * 3.4 mL/min/kg [mild renal function] * 2.7 mL/min/kg [moderate renal function] * 2.8 mL/min/kg [severe renal function] * 1 mL/min/kg [Dialysis-dependent patients] Peptides Organic Compounds Organic Acids Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Angiomax 55154-2275_799d3b00-809b-4abc-989c-05faccec49f8 55154-2275 2000-12-15 injection, powder, lyophilized, for solution 250 mg intravenous NDA020873 false false true US FDA NDC Angiomax 65293-001_3ec737af-bb1b-4479-90a1-081835bae427 65293-001 2000-12-15 injection, powder, lyophilized, for solution 250 mg/5mL intravenous NDA020873 false false true US FDA NDC Angiomax 02246533 powder for solution 250 mg intravenous false false true Canada DPD Angiox Ben Venue Laboratories Inc. http://www.benvenue.com Oryx Pharmaceuticals Inc. Sepracor Pharmaceuticals Inc. http://www.sepracor.com The Medicines Co. http://www.themedicinescompany.com The medicines co Angiomax 250 mg vial 780.0 vial Antithrombins Humans and other mammals

Injection, powder, lyophilized, for solution

intravenous 250 mg

Injection, powder, lyophilized, for solution

intravenous 250 mg/5mL

Powder for solution

intravenous 250 mg BLOOD AND BLOOD FORMING ORGANS ANTITHROMBOTIC AGENTS ANTITHROMBOTIC AGENTS Direct thrombin inhibitors 20:12.04.12 2065150 Canada 1999-12-14 2010-08-17 5196404 United States 1993-05-23 2010-05-23 7582727 United States 2009-01-27 2029-01-27 Dan shen, dong quai, evening primrose oil, gingko, policosanol, willow bark Echinacea DB00054 Abciximab May enhance the anticoagulant effect of other Anticoagulants. DB01418 Acenocoumarol May enhance the anticoagulant effect of other Anticoagulants. DB00945 Acetylsalicylic acid May enhance the anticoagulant effect of Anticoagulants. DB00009 Alteplase May enhance the anticoagulant effect of Anticoagulants. DB00029 Anistreplase May enhance the anticoagulant effect of Anticoagulants. DB06605 Apixaban May enhance the anticoagulant effect of Anticoagulants. DB04272 Citric Acid May enhance the anticoagulant effect of other Anticoagulants. DB06695 Dabigatran etexilate May enhance the anticoagulant effect of Anticoagulants. DB06779 Dalteparin May enhance the anticoagulant effect of other Anticoagulants. DB01254 Dasatinib May enhance the anticoagulant effect of Anticoagulants. DB01609 Deferasirox Anticoagulants may enhance the adverse/toxic effect of Deferasirox. Specifically, the risk for GI ulceration/irritation or GI bleeding may be increased. DB03619 Deoxycholic Acid Anticoagulants may enhance the adverse/toxic effect of Deoxycholic Acid. Specifically, the risk for bleeding or bruising in the treatment area may be increased. DB00304 Desogestrel May diminish the therapeutic effect of Anticoagulants. More specifically, the potential prothrombotic effects of some progestins and progestin-estrogen combinations may counteract anticoagulant effects. DB00266 Dicoumarol May enhance the anticoagulant effect of other Anticoagulants. DB00378 Dydrogesterone May diminish the therapeutic effect of Anticoagulants. More specifically, the potential prothrombotic effects of some progestins and progestin-estrogen combinations may counteract anticoagulant effects. DB00974 Edetic Acid May enhance the anticoagulant effect of other Anticoagulants. DB01225 Enoxaparin May enhance the anticoagulant effect of other Anticoagulants. DB08794 Ethyl biscoumacetate May enhance the anticoagulant effect of other Anticoagulants. DB00569 Fondaparinux sodium May enhance the anticoagulant effect of other Anticoagulants. DB06730 Gestodene May diminish the therapeutic effect of Anticoagulants. More specifically, the potential prothrombotic effects of some progestins and progestin-estrogen combinations may counteract anticoagulant effects. DB01109 Heparin May enhance the anticoagulant effect of other Anticoagulants. DB00078 Ibritumomab Anticoagulants may enhance the adverse/toxic effect of Ibritumomab. Both agents may contribute to an increased risk of bleeding. DB08935 Obinutuzumab Anticoagulants may enhance the adverse/toxic effect of Obinutuzumab. Specifically, the risk of serious bleeding-related events may be increased. DB00498 Phenindione May enhance the anticoagulant effect of other Anticoagulants. DB00946 Phenprocoumon May enhance the anticoagulant effect of other Anticoagulants. DB00396 Progesterone May diminish the therapeutic effect of Anticoagulants. More specifically, the potential prothrombotic effects of some progestins and progestin-estrogen combinations may counteract anticoagulant effects. DB00015 Reteplase May enhance the anticoagulant effect of Anticoagulants. DB01207 Ridogrel May enhance the anticoagulant effect of Anticoagulants. DB06228 Rivaroxaban Anticoagulants may enhance the anticoagulant effect of Rivaroxaban. DB01398 Salicylate-sodium May enhance the anticoagulant effect of Anticoagulants. DB00086 Streptokinase May enhance the anticoagulant effect of Anticoagulants. DB06206 Sugammadex May enhance the anticoagulant effect of Anticoagulants. DB06271 Sulodexide May enhance the anticoagulant effect of other Anticoagulants. DB00031 Tenecteplase May enhance the anticoagulant effect of Anticoagulants. DB00932 Tipranavir May enhance the anticoagulant effect of Anticoagulants. DB00374 Treprostinil May enhance the anticoagulant effect of other Anticoagulants. DB00013 Urokinase May enhance the anticoagulant effect of Anticoagulants. DB00163 Vitamin E May enhance the anticoagulant effect of Anticoagulants. Vitamin E may also increase the overall risk for bleeding. DB09030 Vorapaxar May enhance the adverse/toxic effect of Anticoagulants. More specifically, this combination is expected to increase the risk of bleeding. DB00682 Warfarin May enhance the anticoagulant effect of other Anticoagulants. >Bivalirudin sequence FPRPGGGGNGDFEEIPEEYL Hydrophobicity -0.985 Isoelectric Point 3.91 Molecular Weight 2180.2853 Molecular Formula C98H138N24O33 KEGG Drug D03136 National Drug Code Directory 65293-001-01 PharmGKB PA10032 Wikipedia Bivalirudin RxList http://www.rxlist.com/cgi/generic/angiomax.htm Drugs.com http://www.drugs.com/cdi/bivalirudin.html SMP00277 Bivalirudin Action Pathway DB00006 Bivalirudin DB01022 Phylloquinone 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 # Scatena R: Bivalirudin: a new generation antithrombotic drug. Expert Opin Investig Drugs. 2000 May;9(5):1119-27. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11060732 # Bates ER: Bivalirudin for percutaneous coronary intervention and in acute coronary syndromes. Curr Cardiol Rep. 2001 Sep;3(5):348-54. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11504570 # Gladwell TD: Bivalirudin: a direct thrombin inhibitor. Clin Ther. 2002 Jan;24(1):38-58. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11833835 # Kleiman NS, Klem J, Fernandes LS, Rubin H, Challa S, Solomon S, Maresh K, Arora U, Klem E, Buergler J, Mathew S, Browning A, DeLao T: Pharmacodynamic profile of the direct thrombin antagonist bivalirudin given in combination with the glycoprotein IIb/IIIa antagonist eptifibatide. Am Heart J. 2002 Apr;143(4):585-93. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11923794 # Carswell CI, Plosker GL: Bivalirudin: a review of its potential place in the management of acute coronary syndromes. Drugs. 2002;62(5):841-70. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/11929334 # 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 binding function catalytic activity function thrombin activity function hydrolase activity function calcium ion binding function peptidase activity function ion binding function endopeptidase activity function cation binding function serine-type endopeptidase activity process cellular protein metabolism process organismal physiological process process regulation of body fluids process physiological process process hemostasis process blood coagulation process metabolism process macromolecule metabolism process protein metabolism process proteolysis BE0001075 Myeloperoxidase Human inhibitor # Rudolph V, Rudolph TK, Schopfer FJ, Bonacci G, Lau D, Szocs K, Klinke A, Meinertz T, Freeman BA, Baldus S: Bivalirudin decreases NO bioavailability by vascular immobilization of myeloperoxidase. J Pharmacol Exp Ther. 2008 Nov;327(2):324-31. Epub 2008 Aug 13. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/18701766[ unknown Myeloperoxidase Involved in peroxidase activity Part of the host defense system of polymorphonuclear leukocytes. It is responsible for microbicidal activity against a wide range of organisms. In the stimulated PMN, MPO catalyzes the production of hypohalous acids, primarily hypochlorous acid in physiologic situations, and other toxic intermediates that greatly enhance PMN microbicidal activity MPO 17q23.1 Lysosome None 9.14 83870.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:7218 GenAtlas MPO GeneCards MPO GenBank Gene Database J02694 GenBank Protein Database 189040 UniProtKB P05164 UniProt Accession PERM_HUMAN EC 1.11.1.7 MPO Myeloperoxidase precursor >Myeloperoxidase precursor MGVPFFSSLRCMVDLGPCWAGGLTAEMKLLLALAGLLAILATPQPSEGAAPAVLGEVDTS LVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPMELLSYFKQPVAATRTAVRAADYLH VALDLLERKLRSLWRRPFNVTDVLTPAQLNVLSKSSGCAYQDVGVTCPEQDKYRTITGMC NNRRSPTLGASNRAFVRWLPAEYEDGFSLPYGWTPGVKRNGFPVALARAVSNEIVRFPTD QLTPDQERSLMFMQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPND PRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMSNQL GLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLL REHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYR SYNDSVDPRIANVFTNAFRYGHTLIQPFMFRLDNRYQPMEPNPRVPLSRVFFASWRVVLE GGIDPILRGLMATPAKLNRQNQIAVDEIRERLFEQVMRIGLDLPALNMQRSRDHGLPGYN AWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPL LACIIGTQFRKLRDGDRFWWENEGVFSMQQRQALAQISLPRIICDNTGITTVSKNNIFMS NSYPRDFVNCSTLPALNLASWREAS >2238 bp ATGGGGGTTCCCTTCTTCTCTTCTCTCAGATGCATGGTGGACTTAGGACCTTGCTGGGCT GGGGGTCTCACTGCAGAGATGAAGCTGCTTCTGGCCCTAGCAGGGCTCCTGGCCATTCTG GCCACGCCCCAGCCCTCTGAAGGTGCTGCTCCAGCTGTCCTGGGGGAGGTGGACACCTCG TTGGTGCTGAGCTCCATGGAGGAGGCCAAGCAGCTGGTGGACAAGGCCTACAAGGAGCGG CGGGAAAGCATCAAGCAGCGGCTTCGCAGCGGCTCAGCCAGCCCCATGGAACTCCTATCC TACTTCAAGCAGCCGGTGGCAGCCACCAGGACGGCGGTGAGGGCCGCTGACTACCTGCAC GTGGCTCTAGACCTGCTGGAGAGGAAGCTGCGGTCCCTGTGGCGAAGGCCATTCAATGTC ACTGATGTGCTGACGCCCGCCCAGCTGAATGTGTTGTCCAAGTCAAGCGGCTGCGCCTAC CAGGACGTGGGGGTGACTTGCCCGGAGCAGGACAAATACCGCACCATCACCGGGATGTGC AACAACAGACGCAGCCCCACGCTGGGGGCCTCCAACCGTGCCTTTGTGCGCTGGCTGCCG GCGGAGTATGAGGACGGCTTCTCTCTTCCCTACGGCTGGACGCCCGGGGTCAAGCGCAAC GGCTTCCCGGTGGCTCTGGCTCGCGCGGTCTCCAACGAGATCGTGCGCTTCCCCACTGAT CAGCTGACTCCGGACCAGGAGCGCTCACTCATGTTCATGCAATGGGGCCAGCTGTTGGAC CACGACCTCGACTTCACCCCTGAGCCGGCCGCCCGGGCCTCCTTCGTCACTGGCGTCAAC TGCGAGACCAGCTGCGTTCAGCAGCCGCCCTGCTTCCCGCTCAAGATCCCGCCCAATGAC CCCCGCATCAAGAACCAAGCCGACTGCATCCCGTTCTTCCGCTCCTGCCCGGCTTGCCCC GGGAGCAACATCACCATCCGCAACCAGATCAACGCGCTCACTTCCTTCGTGGACGCCAGC ATGGTGTACGGCAGCGAGGAGCCCCTGGCCAGGAACCTGCGCAACATGTCCAACCAGCTG GGGCTGCTGGCCGTCAACCAGCGCTTCCAAGACAACGGCCGGGCCCTGCTGCCCTTTGAC AACCTGCACGATGACCCCTGTCTCCTCACCAACCGCTCAGCGCGCATCCCCTGCTTCCTG GCAGGGGACACCCGTTCCAGTGAGATGCCCGAGCTCACCTCCATGCACACCCTCTTACTT CGGGAGCACAACCGGCTGGCCACAGAGCTCAAGAGCCTGAACCCTAGGTGGGATGGGGAG AGGCTCTACCAGGAAGCCCGGAAGATCGTGGGGGCCATGGTCCAGATCATCACTTACCGG GACTACCTGCCCCTGGTGCTGGGGCCAACGGCCATGAGGAAGTACCTGCCCACGTACCGT TCCTACAATGACTCAGTGGACCCACGCATCGCCAACGTCTTCACCAATGCCTTCCGCTAC GGCCACACCCTCATCCAACCCTTCATGTTCCGCCTGGACAATCGGTACCAGCCCATGGAA CCCAACCCCCGTGTCCCCCTCAGCAGGGTCTTTTTTGCCTCCTGGAGGGTCGTGCTGGAA GGTGGCATTGACCCCATCCTCCGGGGCCTCATGGCCACCCCTGCCAAGCTGAATCGTCAG AACCAAATTGCAGTGGATGAGATCCGGGAGCGATTGTTTGAGCAGGTCATGAGGATTGGG CTGGACCTGCCTGCTCTGAACATGCAGCGCAGCAGGGACCACGGCCTCCCAGGATACAAT GCCTGGAGGCGCTTCTGTGGGCTCCCGCAGCCTGAAACTGTGGGCCAGCTGGGCACGGTG CTGAGGAACCTGAAATTGGCGAGGAAACTGATGGAGCAGTATGGCACGCCCAACAACATC GACATCTGGATGGGCGGCGTGTCCGAGCCTCTGAAGCGCAAAGGCCGCGTGGGCCCACTC CTCGCCTGCATCATCGGTACCCAGTTCAGGAAGCTCCGGGATGGTGATCGGTTTTGGTGG GAGAACGAGGGTGTGTTCAGCATGCAGCAGCGACAGGCCCTGGCCCAGATCTCATTGCCC CGGATCATCTGCGACAACACAGGCATCACCACCGTGTCTAAGAACAACATCTTCATGTCC AACTCATATCCCCGGGACTTTGTCAACTGCAGTACACTTCCTGCATTGAACCTGGCTTCC TGGAGGGAAGCCTCCTAG PF03098 An_peroxidase function antioxidant activity function peroxidase activity process physiological process process metabolism process cellular metabolism process oxygen and reactive oxygen species metabolism process response to oxidative stress unknown unknown DB00007 BIOD00009 BTD00009 Leuprolide Leuprolide belongs to the general class of drugs known as hormones or hormone antagonists. It is a synthetic 9 residue peptide analog of gonadotropin releasing hormone. Leuprolide is used to treat advanced prostate cancer. It is also used to treat uterine fibroids and endometriosis. Leuprolide is also under investigation for possible use in the treatment of mild to moderate Alzheimer's disease. 53714-56-0 approved investigational # Saleh FM, Niel T, Fishman MJ: Treatment of paraphilia in young adults with leuprolide acetate: a preliminary case report series. J Forensic Sci. 2004 Nov;49(6):1343-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15568711 # Geier MR, Geier DA: The potential importance of steroids in the treatment of autistic spectrum disorders and other disorders involving mercury toxicity. Med Hypotheses. 2005;64(5):946-54. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15780490 # Doraiswamy PM, Xiong GL: Pharmacological strategies for the prevention of Alzheimer's disease. Expert Opin Pharmacother. 2006 Jan;7(1):1-10. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16370917 # Sequence Information "Link":http://www.freepatentsonline.com/EP1790656.html # "RxMed":http://www.rxmed.com/b.main/b2.pharmaceutical/b2.1.monographs/CPS-%20Monographs/CPS-%20(General%20Monographs-%20L)/LUPRON%20DEPOT.html Daniel Kadzimirzs, Gerhard Jas, Volker Autze, "Solution-Phase Synthesis of Leuprolide and Its Intermediates." U.S. Patent US20090005535, issued January 01, 2009. For treatment of prostate cancer, endometriosis, uterine fibroids and premature puberty Used in the palliative treatment of advanced prostate cancer. Leuprolide is a luteinizing hormone agonist that results in suppression of testicular or follicular steroidogenesis. Leuprolide binds to the gonadotropin releasing hormone receptor and acts as a potent inhibitor of gonadotropin secretion. In rats subcutaneous administration of 250 to 500 times the recommended human dose, expressed on a per body weight basis, resulted in dyspnea, decreased activity, and local irritation at the injection site. There is no evidence at present that there is a clinical counterpart of this phenomenon. In early clinical trials with leuprolide acetate doses as high as 20 mg/day for up to two years caused no adverse effects differing from those observed with the 1 mg/day dose. Primarily degraded by peptidase and not by cytochrome P450 enzymes. Bioavailability by subcutaneous administration is comparable to that by intravenous administration. ~3 hours 43% to 49% Excretion in urine * 27 L [intravenous bolus administration to healthy male volunteers] * 8.34 L/h [healthy male receiving a 1-mg IV bolus] Peptides Organic Compounds Organic Acids Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues DBSALT000105 Leuprolide acetate 74381-53-6 InChIKey=RGLRXNKKBLIBQS-XNHQSDQCSA-N (D-Leu(6),des-gly-NH2(10),pro-ethylamide(9))-gonadotropin-releasing hormone L-Pyroglutamyl-L-histidyl-L-tryptophyl-L-seryl-L-tyrosyl-D-leucyl-L-leucyl-L-arginyl-L-proline ethylamide Leuprorelin Leuprorelina Leuproreline Leuprorelinum PGlu-his-trp-ser-tyr-D-leu-leu-arg-pro-NHC2H5 PGlu-his-trp-ser-tyr-D-leu-leu-arg-pro-nhet Eligard 0024-0222_30ed9b7c-a6e6-4f4e-bfb5-396bae4cc4a0 0024-0222 2002-01-23 kit NDA021379 false false true US FDA NDC Eligard 0024-0605_30ed9b7c-a6e6-4f4e-bfb5-396bae4cc4a0 0024-0605 2002-01-23 kit NDA021731 false false true US FDA NDC Eligard 0024-0610_30ed9b7c-a6e6-4f4e-bfb5-396bae4cc4a0 0024-0610 2002-01-23 kit NDA021488 false false true US FDA NDC Eligard 0024-0793_30ed9b7c-a6e6-4f4e-bfb5-396bae4cc4a0 0024-0793 2002-01-23 kit NDA021343 false false true US FDA NDC Leuprolide Acetate 0185-7400_db12d309-92e5-47f0-84d7-aba74956f6e0 0185-7400 1998-08-04 injection, solution 1 mg/.2mL subcutaneous ANDA074728 true false true US FDA NDC Leuprolide Acetate 0781-4003_82a87281-0a93-420c-93e1-1e982b57142f 0781-4003 1998-08-04 kit ANDA074728 true false true US FDA NDC Leuprolide Acetate 41616-936_e08e560f-742e-458e-adf9-037a088a5cfd 41616-936 2009-03-03 kit subcutaneous ANDA078885 true false true US FDA NDC Leuprolide Acetate 47335-936_ade2ad6f-4776-4ad3-a849-8757120a3b07 47335-936 2014-12-15 kit ANDA078885 true false true US FDA NDC Eligard 62935-222_24a44295-5073-434e-af06-a405a6f3ba55 62935-222 2002-01-23 kit subcutaneous NDA021379 false false true US FDA NDC Eligard 62935-302_24a44295-5073-434e-af06-a405a6f3ba55 62935-302 2002-01-23 kit subcutaneous NDA021488 false false true US FDA NDC Eligard 62935-452_24a44295-5073-434e-af06-a405a6f3ba55 62935-452 2002-01-23 kit subcutaneous NDA021731 false false true US FDA NDC Eligard 62935-752_24a44295-5073-434e-af06-a405a6f3ba55 62935-752 2002-01-23 kit subcutaneous NDA021343 false false true US FDA NDC Lupron 00727695 liquid 5 mg subcutaneous false false true Canada DPD Enantone Leuplin Takeda LeuProMaxx Baxter/Teva Leupromer Lutrate Memryte Curaxis Prostap 3 Takeda UK Prostap SR Takeda UK Viadur Bayer AG Abbott Laboratories Ltd. http://www.abbott.com Cardinal Health http://www.cardinal.com Eon Labs Hospira Inc. http://www.hospira.com Oso Biopharmaceuticals Manufacturing LLC Physicians Total Care Inc. http://www.physicianstotalcare.com Sanofi-Aventis Inc. http://www.sanofi-aventis.com Sun Pharmaceutical Industries Ltd. http://www.sunpharma.com Takeda Pharmaceutical Co. Ltd. http://www.takeda.com Teva Pharmaceutical Industries Ltd. http://www.tevapharm.com Tolmar Inc. http://www.tolmar.com Leuprolide 2wk 1 mg/0.2 ml kit 385.33 kit Leuprolide Acetate 1 mg/0.2ml Kit 2.8ml 2-Week Kit 400.74 box Eligard 7.5 mg syringe 493.2 syringe Lupron 2-wk 1 mg/0.2 ml kit 594.37 kit Eligard 22.5 mg syringe 1479.6 syringe Eligard 30 mg syringe 1972.8 syringe Eligard 45 mg syringe 2959.2 syringe Antineoplastic Agents, Hormonal Fertility Agents, Female Estrogen Antagonists Humans and other mammals

Injection, solution

subcutaneous 1 mg/.2mL

Kit

Kit

subcutaneous

Liquid

subcutaneous 5 mg ANTINEOPLASTIC AND IMMUNOMODULATING AGENTS ENDOCRINE THERAPY HORMONES AND RELATED AGENTS Gonadotropin releasing hormone analogues 10:00.00 DB00414 Acetohexamide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB06203 Alogliptin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB08907 Canagliflozin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00672 Chlorpropamide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01120 Gliclazide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00222 Glimepiride Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01251 Gliquidone Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01016 Glyburide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01306 Insulin Aspart Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01307 Insulin Detemir Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00047 Insulin Glargine Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01309 Insulin Glulisine Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00046 Insulin Lispro Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00030 Insulin Regular Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB08914 Insulin, isophane Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB08882 Linagliptin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00331 Metformin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB00834 Mifepristone May enhance the QTc-prolonging effect of Moderate Risk QTc-Prolonging Agents. DB00912 Repaglinide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB06335 Saxagliptin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB01124 Tolbutamide Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. DB04876 Vildagliptin Hyperglycemia-Associated Agents may diminish the therapeutic effect of Antidiabetic Agents. >Leuprolide PHWSYLLR Hydrophobicity 0.1 Molecular Weight 1209.3983 Molecular Formula C59H84N16O12 ChEBI 6427 KEGG Compound C07612 KEGG Drug D08113 National Drug Code Directory 0024-0793-75 PharmGKB PA450203 Wikipedia Leuprolide RxList http://www.rxlist.com/cgi/generic/eligard.htm Drugs.com http://www.drugs.com/cdi/leuprolide.html BE0000203 Gonadotropin-releasing hormone receptor Human agonist # Castellon E, Clementi M, Hitschfeld C, Sanchez C, Benitez D, Saenz L, Contreras H, Huidobro C: Effect of leuprolide and cetrorelix on cell growth, apoptosis, and GnRH receptor expression in primary cell cultures from human prostate carcinoma. Cancer Invest. 2006 Apr-May;24(3):261-8. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/16809153 # Borroni R, Di Blasio AM, Gaffuri B, Santorsola R, Busacca M, Vigano P, Vignali M: Expression of GnRH receptor gene in human ectopic endometrial cells and inhibition of their proliferation by leuprolide acetate. Mol Cell Endocrinol. 2000 Jan 25;159(1-2):37-43. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10687850 # Imai A, Takagi A, Horibe S, Takagi H, Tamaya T: Fas and Fas ligand system may mediate antiproliferative activity of gonadotropin-releasing hormone receptor in endometrial cancer cells. Int J Oncol. 1998 Jul;13(1):97-100. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/9625809 # Murase M, Uemura T, Gao M, Inada M, Funabashi T, Hirahara F: GnRH antagonist-induced down-regulation of the mRNA expression of pituitary receptors: comparisons with GnRH agonist effects. Endocr J. 2005 Feb;52(1):131-7. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/15758569 # Khurana KK, Singh SB, Tatum AH, Schulz V, Badawy SZ: Maintenance of increased Bcl-2 expression in uterine leiomyomas after GnRH agonist therapy. J Reprod Med. 1999 Jun;44(6):487-92. "Pubmed":http://www.ncbi.nlm.nih.gov/pubmed/10394541 yes Gonadotropin-releasing hormone receptor Involved in rhodopsin-like receptor activity Receptor for gonadotropin releasing hormone (GnRH) that mediate the action of GnRH to stimulate the secretion of the gonadotropic hormones (LH and FSH). This receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Isoform 2 may act a an inhibitor of GnRH-R signaling GNRHR 4q21.2 Membrane; multi-pass membrane protein 39-58 78-97 116-137 165-184 213-232 282-300 307-326 9.93 37731.0 Human HUGO Gene Nomenclature Committee (HGNC) HGNC:4421 GenAtlas GNRHR GeneCards GNRHR GenBank Gene Database L03380 GenBank Protein Database 183422 IUPHAR 256 Guide to Pharmacology 31 UniProtKB P30968 UniProt Accession GNRHR_HUMAN GnRH receptor GnRH-R >Gonadotropin-releasing hormone receptor MANSASPEQNQNHCSAINNSIPLMQGNLPTLTLSGKIRVTVTFFLFLLSATFNASFLLKL QKWTQKKEKGKKLSRMKLLLKHLTLANLLETLIVMPLDGMWNITVQWYAGELLCKVLSYL KLFSMYAPAFMMVVISLDRSLAITRPLALKSNSKVGQSMVGLAWILSSVFAGPQLYIFRM IHLADSSGQTKVFSQCVTHCSFSQWWHQAFYNFFTFSCLFIIPLFIMLICNAKIIFTLTR VLHQDPHELQLNQSKNNIPRARLKTLKMTVAFATSFTVCWTPYYVLGIWYWFDPEMLNRL SDPVNHFFFLFAFLNPCFDPLIYGYFSL >987 bp ATGGCAAACAGTGCCTCTCCTGAACAGAATCAAAATCACTGTTCAGCCATCAACAACAGC ATCCCACTGATGCAGGGCAACCTCCCCACTCTGACCTTGTCTGGAAAGATCCGAGTGACG GTTACTTTCTTCCTTTTTCTGCTCTCTGCGACCTTTAATGCTTCTTTCTTGTTGAAACTT CAGAAGTGGACACAGAAGAAAGAGAAAGGGAAAAAGCTCTCAAGAATGAAGCTGCTCTTA AAACATCTGACCTTAGCCAACCTGTTGGAGACTCTGATTGTCATGCCACTGGATGGGATG TGGAACATTACAGTCCAATGGTATGCTGGAGAGTTACTCTGCAAAGTTCTCAGTTATCTA AAGCTTTTCTCCATGTATGCCCCAGCCTTCATGATGGTGGTGATCAGCCTGGACCGCTCC CTGGCTATCACGAGGCCCCTAGCTTTGAAAAGCAACAGCAAAGTCGGACAGTCCATGGTT GGCCTGGCCTGGATCCTCAGTAGTGTCTTTGCAGGACCACAGTTATACATCTTCAGGATG ATTCATCTAGCAGACAGCTCTGGACAGACAAAAGTTTTCTCTCAATGTGTAACACACTGC AGTTTTTCACAATGGTGGCATCAAGCATTTTATAACTTTTTCACCTTCAGCTGCCTCTTC ATCATCCCTCTTTTCATCATGCTGATCTGCAATGCAAAAATCATCTTCACCCTGACACGG GTCCTTCATCAGGACCCCCACGAACTACAACTGAATCAGTCCAAGAACAATATACCAAGA GCACGGCTGAAGACTCTAAAAATGACGGTTGCATTTGCCACTTCATTTACTGTCTGCTGG ACTCCCTACTATGTCCTAGGAATTTGGTATTGGTTTGATCCTGAAATGTTAAACAGGTTG TCAGACCCAGTAAATCACTTCTTCTTTCTCTTTGCCTTTTTAAACCCATGCTTTGATCCA CTTATCTATGGATATTTTTCTCTGTGA PF00001 7tm_1 component cell component intrinsic to membrane component integral to membrane component membrane function protein-hormone receptor activity function signal transducer activity function gonadotropin-releasing hormone receptor activity function receptor activity function transmembrane receptor activity function G-protein coupled receptor activity function rhodopsin-like receptor activity process cellular process process cell communication process signal transduction process cell surface receptor linked signal transduction process G-protein coupled receptor protein signaling pathway DB00008 BIOD00043 BTD00043 Peginterferon alfa-2a Human interferon 2a, is a covalent conjugate of recombinant alfa-2a interferon with a single branched bis-monomethoxy polyethylene glycol (PEG) chain. The PEG moiety is linked at a single site to the interferon alfa moiety via a stable amide bond to lysine. Peginterferon alfa-2a has an approximate molecular weight of 60,000 daltons. Interferon alfa-2a is produced using recombinant DNA technology in which a cloned human leukocyte interferon gene is inserted into and expressed in Escherichia coli. The resultant protein is 165 amino acids. The PEG strand protects the molecule in vivo from proteolytic breakdown, substantially increases its in vivo half-life, and reduces immunogenicity by wrapping around and physically hindering access to the protein portion of the molecule. 198153-51-4 approved investigational For treatment of hairy cell leukemia, malignant melanoma, and AIDS-related Kaposi's sarcoma. Upregulates the expression of MHC I proteins, allowing for increased presentation of peptides derived from viral antigens. This enhances the activation of CD8+ T cells that are the precursors for cytotoxic T lymphocytes (CTLs) and makes the macrophage a better target for CTL-mediated killing. Interferon alpha also induce the synthesis of several key antiviral mediators, including 2'-5' oligoadenylate synthetase (2'-5' A synthetase) and protein kinase R. Interferon alpha binds to type I interferon receptors (IFNAR1 and IFNAR2c) which, upon dimerization, activate two Jak (Janus kinase) tyrosine kinases (Jak1 and Tyk2). These transphosphorylate themselves and phosphorylate the receptors. The phosphorylated INFAR receptors then bind to Stat1 and Stat2 (signal transducers and activators of transcription) which dimerize and activate multiple (~100) immunomodulatory and antiviral proteins. Interferon alpha binds less stably to type I interferon receptors than interferon beta. Terminal half life is 80 hours (range 50 to 140 hours). Peptides Organic Compounds Organic Acids Carboxylic Acids and Derivatives Amino Acids, Peptides, and Analogues Pegasys 0004-0350_d9af3189-1bec-44b8-841c-e96471bb01dd 0004-0350 2002-10-16 injection, solution 180 ug/mL subcutaneous BLA103964 false false true US FDA NDC Pegasys 0004-0357_d9af3189-1bec-44b8-841c-e96471bb01dd 0004-0357 2011-03-29 injection, solution