#BEGIN_DRUGCARD DB00001

# AHFS_Codes:
20:12.04.12

# ATC_Codes:
B01AE02

# Absorption:
Bioavailability is 100% following injection.

# Biotransformation:
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.

# Brand_Mixtures:
Not Available

# Brand_Names:
Refludan

# CAS_Registry_Number:
120993-53-5

# ChEBI_ID:
Not Available

# Chemical_Formula:
C287H440N80O110S6

# Chemical_IUPAC_Name:
Not Available

# Chemical_Structure:
>DB00001 sequence
LVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIP
EEYLQ

# Creation_Date:
2005-06-13 07:24:05 -0600

# DPD_Drug_ID_Number:
02240996

# Description:
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.

# Dosage_Forms:
Powder, for solution	Intravenous

# Drug_Category:
Anticoagulants
Antithrombotic Agents
Fibrinolytic Agents

# Drug_Interactions:
Not Available

# Drug_Reference:
16241940	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.
16244762	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.
16690967	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.

# Drug_Type:
Approved
Biotech

# Experimental_Caco2_Permeability:
Not Available

# Experimental_LogP_Hydrophobicity:
-0.777

# Experimental_Logs:
Not Available

# Experimental_Water_Solubility:
Not Available

# Food_Interactions:
Not Available

# GenBank_ID:
Not Available

# Generic_Name:
Lepirudin

# HET_ID:
Not Available

# Half_Life:
Approximately 1.3 hours

# InChI_Identifier:
Not Available

# InChI_Key:
Not Available

# Indication:
For the treatment of heparin-induced thrombocytopenia

# KEGG_Compound_ID:
Not Available

# KEGG_Drug_ID:
Not Available

# LIMS_Drug_ID:
1

# Mechanism_Of_Action:
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.

# Melting_Point:
65 oC (Otto, A. & Seckler, R. Eur. J. Biochem. 202:67-73 (1991))

# Molecular_Weight_Avg:
6963.4250

# Molecular_Weight_Mono:
Not Available

# Organisms_Affected:
Humans and other mammals

# PDB_Experimental_ID:
4HIR

# PDB_Homology_ID:
Not Available

# PDRhealth_Link:
Not Available

# Pathways:
Lepirudin Pathway	SMP00278

# PharmGKB_ID:
PA450195

# Pharmacology:
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.

# Predicted_LogP_Hydrophobicity:
Not Available

# Predicted_LogS:
Not Available

# Predicted_Water_Solubility:
Not Available

# Primary_Accession_No:
DB00001

# Protein_Binding:
Not Available

# PubChem_Compound_ID:
Not Available

# PubChem_Substance_ID:
Not Available

# RxList_Link:
http://www.rxlist.com/cgi/generic/lepirudin.htm

# Secondary_Accession_No:
BIOD00024
BTD00024

# Smiles_String_canonical:
Not Available

# Smiles_String_isomeric:
Not Available

# State:
liquid

# Structure:
0

# SwissProt_ID:
P01050

# SwissProt_Name:
ITH1_HIRME

# Synonyms:
Hirudin variant-1

# Synthesis_Reference:
Not Available

# Toxicity:
In case of overdose (eg, suggested by excessively high aPTT values) the risk of bleeding is increased.

# Update_Date:
2011-06-15 11:49:16 -0600

# Wikipedia_Link:
http://en.wikipedia.org/wiki/Lepirudin

# pKa_Isoelectric_Point:
4.04

# Drug_Target_1_Cellular_Location:
Secreted protein
extracellular space

# Drug_Target_1_Chromosome_Location:
Not Available

# Drug_Target_1_Drug_References:
10505536	Turpie AG: Anticoagulants in acute coronary syndromes. Am J Cardiol. 1999 Sep 2;84(5A):2M-6M.
10912644	Warkentin TE: Venous thromboembolism in heparin-induced thrombocytopenia. Curr Opin Pulm Med. 2000 Jul;6(4):343-51.
11055889	Eriksson BI: New therapeutic options in deep vein thrombosis prophylaxis. Semin Hematol. 2000 Jul;37(3 Suppl 5):7-9.
11467439	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.
11752352	Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5.
11807012	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.

# Drug_Target_1_Essentiality:
Non-Essential

# Drug_Target_1_GenAtlas_ID:
F2

# Drug_Target_1_GenBank_ID_Gene:
M17262

# Drug_Target_1_GenBank_ID_Protein:
339641

# Drug_Target_1_GeneCard_ID:
F2

# Drug_Target_1_Gene_Name:
F2

# Drug_Target_1_Gene_Sequence:
>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

# Drug_Target_1_General_Function:
Involved in blood clotting cascade

# Drug_Target_1_General_References:
10051558	Guinto ER, Caccia S, Rose T, Futterer K, Waksman G, Di Cera E: Unexpected crucial role of residue 225 in serine proteases. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):1852-7.
10391209	Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8.
1349838	Iwahana H, Yoshimoto K, Shigekiyo T, Shirakami A, Saito S, Itakura M: Detection of a single base substitution of the gene for prothrombin Tokushima. The application of PCR-SSCP for the genetic and molecular analysis of dysprothrombinemia. Int J Hematol. 1992 Feb;55(1):93-100.
1354985	Miyata T, Aruga R, Umeyama H, Bezeaud A, Guillin MC, Iwanaga S: Prothrombin Salakta: substitution of glutamic acid-466 by alanine reduces the fibrinogen clotting activity and the esterase activity. Biochemistry. 1992 Aug 25;31(33):7457-62.
1421398	Morishita E, Saito M, Kumabashiri I, Asakura H, Matsuda T, Yamaguchi K: Prothrombin Himi: a compound heterozygote for two dysfunctional prothrombin molecules (Met-337-->Thr and Arg-388-->His). Blood. 1992 Nov 1;80(9):2275-80.
2374926	Rydel TJ, Ravichandran KG, Tulinsky A, Bode W, Huber R, Roitsch C, Fenton JW 2nd: The structure of a complex of recombinant hirudin and human alpha-thrombin. Science. 1990 Jul 20;249(4966):277-80.
2583108	Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J: The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989 Nov;8(11):3467-75.
266717	Walz DA, Hewett-Emmett D, Seegers WH: Amino acid sequence of human prothrombin fragments 1 and 2. Proc Natl Acad Sci U S A. 1977 May;74(5):1969-72.
2719946	Henriksen RA, Mann KG: Substitution of valine for glycine-558 in the congenital dysthrombin thrombin Quick II alters primary substrate specificity. Biochemistry. 1989 Mar 7;28(5):2078-82.
2825773	Degen SJ, Davie EW: Nucleotide sequence of the gene for human prothrombin. Biochemistry. 1987 Sep 22;26(19):6165-77.
3242619	Henriksen RA, Mann KG: Identification of the primary structural defect in the dysthrombin thrombin Quick I: substitution of cysteine for arginine-382. Biochemistry. 1988 Dec 27;27(26):9160-5.
3567158	Miyata T, Morita T, Inomoto T, Kawauchi S, Shirakami A, Iwanaga S: Prothrombin Tokushima, a replacement of arginine-418 by tryptophan that impairs the fibrinogen clotting activity of derived thrombin Tokushima. Biochemistry. 1987 Feb 24;26(4):1117-22.
3759958	Rabiet MJ, Blashill A, Furie B, Furie BC: Prothrombin fragment 1 X 2 X 3, a major product of prothrombin activation in human plasma. J Biol Chem. 1986 Oct 5;261(28):13210-5.
3771562	Rabiet MJ, Furie BC, Furie B: Molecular defect of prothrombin Barcelona. Substitution of cysteine for arginine at residue 273. J Biol Chem. 1986 Nov 15;261(32):15045-8.
3801671	Inomoto T, Shirakami A, Kawauchi S, Shigekiyo T, Saito S, Miyoshi K, Morita T, Iwanaga S: Prothrombin Tokushima: characterization of dysfunctional thrombin derived from a variant of human prothrombin. Blood. 1987 Feb;69(2):565-9.
6305407	Degen SJ, MacGillivray RT, Davie EW: Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin. Biochemistry. 1983 Apr 26;22(9):2087-97.
6405779	Board PG, Shaw DC: Determination of the amino acid substitution in human prothrombin type 3 (157 Glu leads to Lys) and the localization of a third thrombin cleavage site. Br J Haematol. 1983 Jun;54(2):245-54.
7792730	Degen SJ, McDowell SA, Sparks LM, Scharrer I: Prothrombin Frankfurt: a dysfunctional prothrombin characterized by substitution of Glu-466 by Ala. Thromb Haemost. 1995 Feb;73(2):203-9.
7865694	James HL, Kim DJ, Zheng DQ, Girolami A: Prothrombin Padua I: incomplete activation due to an amino acid substitution at a factor Xa cleavage site. Blood Coagul Fibrinolysis. 1994 Oct;5(5):841-4.
8071320	Rydel TJ, Yin M, Padmanabhan KP, Blankenship DT, Cardin AD, Correa PE, Fenton JW 2nd, Tulinsky A: Crystallographic structure of human gamma-thrombin. J Biol Chem. 1994 Sep 2;269(35):22000-6.
873923	Butkowski RJ, Elion J, Downing MR, Mann KG: Primary structure of human prethrombin 2 and alpha-thrombin. J Biol Chem. 1977 Jul 25;252(14):4942-57.
9214615	van de Locht A, Bode W, Huber R, Le Bonniec BF, Stone SR, Esmon CT, Stubbs MT: The thrombin E192Q-BPTI complex reveals gross structural rearrangements: implications for the interaction with antithrombin and thrombomodulin. EMBO J. 1997 Jun 2;16(11):2977-84.

# Drug_Target_1_HGNC_ID:
HGNC:3535

# Drug_Target_1_HPRD_ID:
01488

# Drug_Target_1_ID:
54

# Drug_Target_1_Locus:
11p11-q12

# Drug_Target_1_Molecular_Weight:
70037

# Drug_Target_1_Name:
Prothrombin

# Drug_Target_1_Number_of_Residues:
632

# Drug_Target_1_PDB_ID:
1HAG

# Drug_Target_1_Pathway:
Abciximab Pathway	SMP00265
Acenocoumarol Pathway	SMP00269
Acetylsalicylic Acid Pathway	SMP00083
Alteplase Pathway	SMP00280
Aminocaproic Acid Pathway	SMP00286
Anistreplase Pathway	SMP00281
Aprotinin Pathway	SMP00288
Ardeparin Pathway	SMP00275
Argatroban Pathway	SMP00276
Bivalirudin Pathway	SMP00277
Celecoxib Pathway	SMP00096
Cilostazol Pathway	SMP00263
Clopidogrel Pathway	SMP00260
Dicumarol Pathway	SMP00270
Dipyridamole (Antiplatelet) Pathway	SMP00264
Enoxaparin Pathway	SMP00272
Eptifibatide Pathway	SMP00266
Etodolac Pathway	SMP00084
Fondaparinux Pathway	SMP00273
Heparin Pathway	SMP00274
Lepirudin Pathway	SMP00278
Meloxicam Pathway	SMP00106
Phenprocoumon Pathway	SMP00271
Reteplase Pathway	SMP00285
Rofecoxib Pathway	SMP00087
Streptokinase Pathway	SMP00282
Tenecteplase Pathway	SMP00283
Ticlopidine Pathway	SMP00261
Tirofiban Pathway	SMP00267
Tranexamic Acid Pathway	SMP00287
Urokinase Pathway	SMP00284
Valdecoxib Pathway	SMP00116
Warfarin Pathway	SMP00268
Ximelagatran Pathway	SMP00279

# Drug_Target_1_Pfam_Domain_Function:
PF00051	Kringle
PF00089	Trypsin
PF00594	Gla

# Drug_Target_1_Protein_Sequence:
>Prothrombin precursor
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE

# Drug_Target_1_Reaction:
Selective cleavage of Arg!Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B INHIBITOR Benzamidine; D-Phe-Pro-Arg-CH2Cl; Nalpha-(2-naphthyl-sulfonyl-glycyl)-D-p-amidinopheyl-alanylpiperadin e; Argatroban

# Drug_Target_1_Signals:
1-24

# Drug_Target_1_Specific_Function:
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

# Drug_Target_1_SwissProt_ID:
P00734

# Drug_Target_1_SwissProt_Name:
THRB_HUMAN

# Drug_Target_1_Synonyms:
Activated Factor II [IIa]
Coagulation factor II
EC 3.4.21.5
Prothrombin precursor
Thrombin

# Drug_Target_1_Theoretical_pI:
5.70

# Drug_Target_1_Transmembrane_Regions:
None

#END_DRUGCARD DB00001
#BEGIN_DRUGCARD DB00002

# AHFS_Codes:
Not Available

# ATC_Codes:
L01XC06

# Absorption:
Not Available

# Biotransformation:
Not Available

# Brand_Mixtures:
Not Available

# Brand_Names:
Erbitux

# CAS_Registry_Number:
205923-56-4

# ChEBI_ID:
Not Available

# Chemical_Formula:
C6484H10042N1732O2023S36

# Chemical_IUPAC_Name:
Not Available

# Chemical_Structure:
>Anti-EGFR heavy chain 1
QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYN
TPFTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAA
STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG
LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSPKSCDKTHTCPPCPAPELL
GGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQ
YNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR
DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS
RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
>Anti-EGFR heavy chain 2
QVQLKQSGPGLVQPSQSLSITCTVSGFSLTNYGVHWVRQSPGKGLEWLGVIWSGGNTDYN
TPFTSRLSINKDNSKSQVFFKMNSLQSNDTAIYYCARALTYYDYEFAYWGQGTLVTVSAA
STKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSG
LYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKRVEPKSPKSCDKTHTCPPCPAPELL
GGPSVFLFPPKPKDTLMISRTPEVTCVVVDVSHEDPEVKFNWYVDGVEVHNAKTKPREEQ
YNSTYRVVSVLTVLHQDWLNGKEYKCKVSNKALPAPIEKTISKAKGQPREPQVYTLPPSR
DELTKNQVSLTCLVKGFYPSDIAVEWESNGQPENNYKTTPPVLDSDGSFFLYSKLTVDKS
RWQQGNVFSCSVMHEALHNHYTQKSLSLSPGK
>Anti-EGFR light chain 1
DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPS
RFSGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGA
>Anti-EGFR light chain 2
DILLTQSPVILSVSPGERVSFSCRASQSIGTNIHWYQQRTNGSPRLLIKYASESISGIPS
RFSGSGSGTDFTLSINSVESEDIADYYCQQNNNWPTTFGAGTKLELKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGA

# Creation_Date:
2005-06-13 07:24:05 -0600

# DPD_Drug_ID_Number:
Not Available

# Description:
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.

# Dosage_Forms:
Solution	Intravenous

# Drug_Category:
Antineoplastic Agents

# Drug_Interactions:
Not Available

# Drug_Reference:
Not Available

# Drug_Type:
Approved
Biotech

# Experimental_Caco2_Permeability:
Not Available

# Experimental_LogP_Hydrophobicity:
-0.413

# Experimental_Logs:
Not Available

# Experimental_Water_Solubility:
Not Available

# Food_Interactions:
Not Available

# GenBank_ID:
J00228

# Generic_Name:
Cetuximab

# HET_ID:
Not Available

# Half_Life:
114 hrs

# InChI_Identifier:
Not Available

# InChI_Key:
Not Available

# Indication:
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.

# KEGG_Compound_ID:
Not Available

# KEGG_Drug_ID:
Not Available

# LIMS_Drug_ID:
2

# Mechanism_Of_Action:
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.

# Melting_Point:
61 oC (FAB fragment), 71 oC (whole mAb) - Vermeer, A.W.P. & Norde, W., Biophys. J. 78:394-404 (2000).

# Molecular_Weight_Avg:
145781.6000

# Molecular_Weight_Mono:
Not Available

# Organisms_Affected:
Humans and other mammals

# PDB_Experimental_ID:
1IGT

# PDB_Homology_ID:
Not Available

# PDRhealth_Link:
Not Available

# Pathways:
Cetuximab Pathway	SMP00474

# PharmGKB_ID:
PA10040

# Pharmacology:
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.

# Predicted_LogP_Hydrophobicity:
Not Available

# Predicted_LogS:
Not Available

# Predicted_Water_Solubility:
Not Available

# Primary_Accession_No:
DB00002

# Protein_Binding:
Not Available

# PubChem_Compound_ID:
Not Available

# PubChem_Substance_ID:
Not Available

# RxList_Link:
http://www.rxlist.com/cgi/generic3/erbitux.htm

# Secondary_Accession_No:
BIOD00071
BTD00071

# Smiles_String_canonical:
Not Available

# Smiles_String_isomeric:
Not Available

# State:
liquid

# Structure:
0

# SwissProt_ID:
Not Available

# SwissProt_Name:
Not Available

# Synonyms:
Anti EGFR
IMC-C225
cetuximab

# Synthesis_Reference:
Not Available

# Toxicity:
Single doses of cetuximab higher than 500 mg/m<sup>2</sup> have not been tested. There is no experience with overdosage in human clinical trials.

# Update_Date:
2011-01-04 14:50:20 -0700

# Wikipedia_Link:
http://en.wikipedia.org/wiki/Cetuximab

# pKa_Isoelectric_Point:
8.48

# Drug_Target_10_Cellular_Location:
Membrane

# Drug_Target_10_Chromosome_Location:
Not Available

# Drug_Target_10_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.
17704420	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.

# Drug_Target_10_Essentiality:
Non-Essential

# Drug_Target_10_GenAtlas_ID:
FCGR2A

# Drug_Target_10_GenBank_ID_Gene:
M31932

# Drug_Target_10_GenBank_ID_Protein:
182474

# Drug_Target_10_GeneCard_ID:
FCGR2A

# Drug_Target_10_Gene_Name:
FCGR2A

# Drug_Target_10_Gene_Sequence:
>954 bp
ATGGCTATGGAGACCCAAATGTCTCAGAATGTATGTCCCAGAAACCTGTGGCTGCTTCAA
CCATTGACAGTTTTGCTGCTGCTGGCTTCTGCAGACAGTCAAGCTGCAGCTCCCCCAAAG
GCTGTGCTGAAACTTGAGCCCCCGTGGATCAACGTGCTCCAGGAGGACTCTGTGACTCTG
ACATGCCAGGGGGCTCGCAGCCCTGAGAGCGACTCCATTCAGTGGTTCCACAATGGGAAT
CTCATTCCCACCCACACGCAGCCCAGCTACAGGTTCAAGGCCAACAACAATGACAGCGGG
GAGTACACGTGCCAGACTGGCCAGACCAGCCTCAGCGACCCTGTGCATCTGACTGTGCTT
TCCGAATGGCTGGTGCTCCAGACCCCTCACCTGGAGTTCCAGGAGGGAGAAACCATCATG
CTGAGGTGCCACAGCTGGAAGGACAAGCCTCTGGTCAAGGTCACATTCTTCCAGAATGGA
AAATCCCAGAAATTCTCCCGTTTGGATCCCACCTTCTCCATCCCACAAGCAAACCACAGT
CACAGTGGTGATTACCACTGCACAGGAAACATAGGCTACACGCTGTTCTCATCCAAGCCT
GTGACCATCACTGTCCAAGTGCCCAGCATGGGCAGCTCTTCACCAATGGGGATCATTGTG
GCTGTGGTCATTGCGACTGCTGTAGCAGCCATTGTTGCTGCTGTAGTGGCCTTGATCTAC
TGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTGAAGGCTGCCCAATTTGAG
CCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACTTGAAGAAACCAACAATGAC
TATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGGGCACCTACTGACGATGAT
AAAAACATCTACCTGACTCTTCCTCCCAACGACCATGTCAACAGTAATAACTAA

# Drug_Target_10_General_Function:
Not Available

# Drug_Target_10_General_References:
10331870	Maxwell KF, Powell MS, Hulett MD, Barton PA, McKenzie IF, Garrett TP, Hogarth PM: Crystal structure of the human leukocyte Fc receptor, Fc gammaRIIa. Nat Struct Biol. 1999 May;6(5):437-42.
10397151	Powell MS, Barton PA, Emmanouilidis D, Wines BD, Neumann GM, Peitersz GA, Maxwell KF, Garrett TP, Hogarth PM: Biochemical analysis and crystallisation of Fc gamma RIIa, the low affinity receptor for IgG. Immunol Lett. 1999 May 3;68(1):17-23.
2526077	Seki T: Identification of multiple isoforms of the low-affinity human IgG Fc receptor. Immunogenetics. 1989;30(1):5-12.
2529342	Brooks DG, Qiu WQ, Luster AD, Ravetch JV: Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes. J Exp Med. 1989 Oct 1;170(4):1369-85.
2824655	Stuart SG, Trounstine ML, Vaux DJ, Koch T, Martens CL, Mellman I, Moore KW: Isolation and expression of cDNA clones encoding a human receptor for IgG (Fc gamma RII). J Exp Med. 1987 Dec 1;166(6):1668-84.
2965389	Hibbs ML, Bonadonna L, Scott BM, McKenzie IF, Hogarth PM: Molecular cloning of a human immunoglobulin G Fc receptor. Proc Natl Acad Sci U S A. 1988 Apr;85(7):2240-4.
3402431	Stengelin S, Stamenkovic I, Seed B: Isolation of cDNAs for two distinct human Fc receptors by ligand affinity cloning. EMBO J. 1988 Apr;7(4):1053-9.
8636449	Salmon JE, Millard S, Schachter LA, Arnett FC, Ginzler EM, Gourley MF, Ramsey-Goldman R, Peterson MG, Kimberly RP: Fc gamma RIIA alleles are heritable risk factors for lupus nephritis in African Americans. J Clin Invest. 1996 Mar 1;97(5):1348-54.

# Drug_Target_10_HGNC_ID:
HGNC:3616

# Drug_Target_10_HPRD_ID:
Not Available

# Drug_Target_10_ID:
3819

# Drug_Target_10_Locus:
1q23

# Drug_Target_10_Molecular_Weight:
34990

# Drug_Target_10_Name:
Low affinity immunoglobulin gamma Fc region receptor II-a

# Drug_Target_10_Number_of_Residues:
322

# Drug_Target_10_PDB_ID:
1H9V

# Drug_Target_10_Pathway:
Not Available

# Drug_Target_10_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_10_Protein_Sequence:
>Low affinity immunoglobulin gamma Fc region receptor II-a
MAMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTL
TCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVL
SEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSRLDPTFSIPQANHS
HSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIY
CRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDD
KNIYLTLPPNDHVNSNN

# Drug_Target_10_Reaction:
Not Available

# Drug_Target_10_Signals:
1-33

# Drug_Target_10_Specific_Function:
Binds to the Fc region of immunoglobulins gamma. Low affinity receptor. By binding to IgG it initiates cellular responses against pathogens and soluble antigens

# Drug_Target_10_SwissProt_ID:
P12318

# Drug_Target_10_SwissProt_Name:
FCG2A_HUMAN

# Drug_Target_10_Synonyms:
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

# Drug_Target_10_Theoretical_pI:
6.78

# Drug_Target_10_Transmembrane_Regions:
218-240

# Drug_Target_11_Cellular_Location:
Membrane

# Drug_Target_11_Chromosome_Location:
Not Available

# Drug_Target_11_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_11_Essentiality:
Non-Essential

# Drug_Target_11_GenAtlas_ID:
FCGR2B

# Drug_Target_11_GenBank_ID_Gene:
U87560

# Drug_Target_11_GenBank_ID_Protein:
4099445

# Drug_Target_11_GeneCard_ID:
FCGR2B

# Drug_Target_11_Gene_Name:
FCGR2B

# Drug_Target_11_Gene_Sequence:
>930 bp
ATGGGAATCCTGTCATTCTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG
TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT
GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC
GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC
TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG
TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC
AGCGACCCTGTGCATCTGACTGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG
GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG
GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC
TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCACTGCACAGGAAACATA
GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA
CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCGGCCATTGTTGCTGCT
GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCTCTCCCAGGATACCCTGAG
TGCAGGGAAATGGGAGAGACCCTCCCTGAGAAACCAGCCAATCCCACTAATCCTGATGAG
GCTGACAAAGTTGGGGCTGAGAACACAATCACCTATTCACTTCTCATGCACCCGGATGCT
CTGGAAGAGCCTGATGACCAGAACCGTATT

# Drug_Target_11_General_Function:
Not Available

# Drug_Target_11_General_References:
12115230	Kyogoku C, Dijstelbloem HM, Tsuchiya N, Hatta Y, Kato H, Yamaguchi A, Fukazawa T, Jansen MD, Hashimoto H, van de Winkel JG, Kallenberg CG, Tokunaga K: Fcgamma receptor gene polymorphisms in Japanese patients with systemic lupus erythematosus: contribution of FCGR2B to genetic susceptibility. Arthritis Rheum. 2002 May;46(5):1242-54.
2142460	Engelhardt W, Geerds C, Frey J: Distribution, inducibility and biological function of the cloned and expressed human beta Fc receptor II. Eur J Immunol. 1990 Jun;20(6):1367-77.
2529342	Brooks DG, Qiu WQ, Luster AD, Ravetch JV: Structure and expression of human IgG FcRII(CD32). Functional heterogeneity is encoded by the alternatively spliced products of multiple genes. J Exp Med. 1989 Oct 1;170(4):1369-85.
2531080	Stuart SG, Simister NE, Clarkson SB, Kacinski BM, Shapiro M, Mellman I: Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium. EMBO J. 1989 Dec 1;8(12):3657-66.

# Drug_Target_11_HGNC_ID:
HGNC:3618

# Drug_Target_11_HPRD_ID:
Not Available

# Drug_Target_11_ID:
3820

# Drug_Target_11_Locus:
1q23

# Drug_Target_11_Molecular_Weight:
34044

# Drug_Target_11_Name:
Low affinity immunoglobulin gamma Fc region receptor II-b

# Drug_Target_11_Number_of_Residues:
315

# Drug_Target_11_PDB_ID:
2FCB

# Drug_Target_11_Pathway:
Not Available

# Drug_Target_11_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_11_Protein_Sequence:
>Low affinity immunoglobulin gamma Fc region receptor II-b
MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN
VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL
SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN
FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA
VVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDA
LEEPDDQNRI

# Drug_Target_11_Reaction:
Not Available

# Drug_Target_11_Signals:
1-42

# Drug_Target_11_Specific_Function:
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

# Drug_Target_11_SwissProt_ID:
P31994

# Drug_Target_11_SwissProt_Name:
FCG2B_HUMAN

# Drug_Target_11_Synonyms:
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

# Drug_Target_11_Theoretical_pI:
6.12

# Drug_Target_11_Transmembrane_Regions:
218-240

# Drug_Target_12_Cellular_Location:
Cell membrane

# Drug_Target_12_Chromosome_Location:
Not Available

# Drug_Target_12_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_12_Essentiality:
Non-Essential

# Drug_Target_12_GenAtlas_ID:
FCGR2C

# Drug_Target_12_GenBank_ID_Gene:
X17652

# Drug_Target_12_GenBank_ID_Protein:
32074

# Drug_Target_12_GeneCard_ID:
FCGR2C

# Drug_Target_12_Gene_Name:
FCGR2C

# Drug_Target_12_Gene_Sequence:
>972 bp
ATGGGAATCCTGTCATTTTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG
TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT
GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC
GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC
TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG
TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC
AGCGACCCTGTGCATCTGACAGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG
GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG
GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC
TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCATTGCACAGGAAACATA
GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA
CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCTGCCATTGTTGCTGCT
GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTG
AAGGCTGCCCAATTTGAGCCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACCT
GAAGAAACCAACAATGACTATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGG
GCACCTACTGACGATGATAAAAACATCTACTTGACTCTTCCTCCCAACGACCATGTCAAC
AGTAATAACTAA

# Drug_Target_12_General_Function:
Not Available

# Drug_Target_12_General_References:
2531080	Stuart SG, Simister NE, Clarkson SB, Kacinski BM, Shapiro M, Mellman I: Human IgG Fc receptor (hFcRII; CD32) exists as multiple isoforms in macrophages, lymphocytes and IgG-transporting placental epithelium. EMBO J. 1989 Dec 1;8(12):3657-66.
9516136	Metes D, Ernst LK, Chambers WH, Sulica A, Herberman RB, Morel PA: Expression of functional CD32 molecules on human NK cells is determined by an allelic polymorphism of the FcgammaRIIC gene. Blood. 1998 Apr 1;91(7):2369-80.

# Drug_Target_12_HGNC_ID:
HGNC:15626

# Drug_Target_12_HPRD_ID:
Not Available

# Drug_Target_12_ID:
3821

# Drug_Target_12_Locus:
1q23.3

# Drug_Target_12_Molecular_Weight:
35578

# Drug_Target_12_Name:
Low affinity immunoglobulin gamma Fc region receptor II-c

# Drug_Target_12_Number_of_Residues:
328

# Drug_Target_12_PDB_ID:
2FCB

# Drug_Target_12_Pathway:
Not Available

# Drug_Target_12_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_12_Protein_Sequence:
>Low affinity immunoglobulin gamma Fc region receptor II-c
MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN
VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL
SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN
FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA
VVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQPEETNNDYETADGGYMTLNPR
APTDDDKNIYLTLPPNDHVNSNN

# Drug_Target_12_Reaction:
Not Available

# Drug_Target_12_Signals:
1-42

# Drug_Target_12_Specific_Function:
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

# Drug_Target_12_SwissProt_ID:
P31995

# Drug_Target_12_SwissProt_Name:
FCG2C_HUMAN

# Drug_Target_12_Synonyms:
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

# Drug_Target_12_Theoretical_pI:
6.90

# Drug_Target_12_Transmembrane_Regions:
224-246

# Drug_Target_1_Cellular_Location:
Cell membrane
single-pass type I membrane protein. Isoform 2:Secreted protein

# Drug_Target_1_Chromosome_Location:
Not Available

# Drug_Target_1_Drug_References:
10480573	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.
10601294	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.
10628369	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.
11408594	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.
11431346	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.
11752352	Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5.

# Drug_Target_1_Essentiality:
Non-Essential

# Drug_Target_1_GenAtlas_ID:
EGFR

# Drug_Target_1_GenBank_ID_Gene:
X00588

# Drug_Target_1_GenBank_ID_Protein:
757924

# Drug_Target_1_GeneCard_ID:
EGFR

# Drug_Target_1_Gene_Name:
EGFR

# Drug_Target_1_Gene_Sequence:
>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

# Drug_Target_1_General_Function:
Involved in transmembrane receptor protein tyrosine kinase activity

# Drug_Target_1_General_References:
10731668	Sato C, Kim JH, Abe Y, Saito K, Yokoyama S, Kohda D: Characterization of the N-oligosaccharides attached to the atypical Asn-X-Cys sequence of recombinant human epidermal growth factor receptor. J Biochem (Tokyo). 2000 Jan;127(1):65-72.
11116146	Habib AA, Chatterjee S, Park SK, Ratan RR, Lefebvre S, Vartanian T: The epidermal growth factor receptor engages receptor interacting protein and nuclear factor-kappa B (NF-kappa B)-inducing kinase to activate NF-kappa B. Identification of a novel receptor-tyrosine kinase signalosome. J Biol Chem. 2001 Mar 23;276(12):8865-74. Epub 2000 Dec 14.
11161793	Reiter JL, Threadgill DW, Eley GD, Strunk KE, Danielsen AJ, Sinclair CS, Pearsall RS, Green PJ, Yee D, Lampland AL, Balasubramaniam S, Crossley TD, Magnuson TR, James CD, Maihle NJ: Comparative genomic sequence analysis and isolation of human and mouse alternative EGFR transcripts encoding truncated receptor isoforms. Genomics. 2001 Jan 1;71(1):1-20.
1988448	Haley JD, Waterfield MD: Contributory effects of de novo transcription and premature transcript termination in the regulation of human epidermal growth factor receptor proto-oncogene RNA synthesis. J Biol Chem. 1991 Jan 25;266(3):1746-53.
2543678	Margolis BL, Lax I, Kris R, Dombalagian M, Honegger AM, Howk R, Givol D, Ullrich A, Schlessinger J: All autophosphorylation sites of epidermal growth factor (EGF) receptor and HER2/neu are located in their carboxyl-terminal tails. Identification of a novel site in EGF receptor. J Biol Chem. 1989 Jun 25;264(18):10667-71.
2790960	Chen WS, Lazar CS, Lund KA, Welsh JB, Chang CP, Walton GM, Der CJ, Wiley HS, Gill GN, Rosenfeld MG: Functional independence of the epidermal growth factor receptor from a domain required for ligand-induced internalization and calcium regulation. Cell. 1989 Oct 6;59(1):33-43.
2985580	Russo MW, Lukas TJ, Cohen S, Staros JV: Identification of residues in the nucleotide binding site of the epidermal growth factor receptor/kinase. J Biol Chem. 1985 May 10;260(9):5205-8.
2991899	Ishii S, Xu YH, Stratton RH, Roe BA, Merlino GT, Pastan I: Characterization and sequence of the promoter region of the human epidermal growth factor receptor gene. Proc Natl Acad Sci U S A. 1985 Aug;82(15):4920-4.
3039909	Carpenter G: Receptors for epidermal growth factor and other polypeptide mitogens. Annu Rev Biochem. 1987;56:881-914.
3138233	Heisermann GJ, Gill GN: Epidermal growth factor receptor threonine and serine residues phosphorylated in vivo. J Biol Chem. 1988 Sep 15;263(26):13152-8.
3329716	Haley J, Whittle N, Bennet P, Kinchington D, Ullrich A, Waterfield M: The human EGF receptor gene: structure of the 110 kb locus and identification of sequences regulating its transcription. Oncogene Res. 1987 Sep-Oct;1(4):375-96.
6093780	Simmen FA, Gope ML, Schulz TZ, Wright DA, Carpenter G, O'Malley BW: Isolation of an evolutionarily conserved epidermal growth factor receptor cDNA from human A431 carcinoma cells. Biochem Biophys Res Commun. 1984 Oct 15;124(1):125-32.
6324343	Weber W, Gill GN, Spiess J: Production of an epidermal growth factor receptor-related protein. Science. 1984 Apr 20;224(4646):294-7.
6325948	Mroczkowski B, Mosig G, Cohen S: ATP-stimulated interaction between epidermal growth factor receptor and supercoiled DNA. Nature. 1984 May 17-23;309(5965):270-3.
6326261	Lin CR, Chen WS, Kruiger W, Stolarsky LS, Weber W, Evans RM, Verma IM, Gill GN, Rosenfeld MG: Expression cloning of human EGF receptor complementary DNA: gene amplification and three related messenger RNA products in A431 cells. Science. 1984 May 25;224(4651):843-8.
6328312	Ullrich A, Coussens L, Hayflick JS, Dull TJ, Gray A, Tam AW, Lee J, Yarden Y, Libermann TA, Schlessinger J, et al.: Human epidermal growth factor receptor cDNA sequence and aberrant expression of the amplified gene in A431 epidermoid carcinoma cells. Nature. 1984 May 31-Jun 6;309(5967):418-25.
6330563	Xu YH, Ishii S, Clark AJ, Sullivan M, Wilson RK, Ma DP, Roe BA, Merlino GT, Pastan I: Human epidermal growth factor receptor cDNA is homologous to a variety of RNAs overproduced in A431 carcinoma cells. Nature. 1984 Jun 28-Jul 4;309(5971):806-10.
7654368	Ilekis JV, Stark BC, Scoccia B: Possible role of variant RNA transcripts in the regulation of epidermal growth factor receptor expression in human placenta. Mol Reprod Dev. 1995 Jun;41(2):149-56.
8918811	Reiter JL, Maihle NJ: A 1.8 kb alternative transcript from the human epidermal growth factor receptor gene encodes a truncated form of the receptor. Nucleic Acids Res. 1996 Oct 15;24(20):4050-6.
8962717	Smith KD, Davies MJ, Bailey D, Renouf DV, Hounsell EF: Analysis of the glycosylation patterns of the extracellular domain of the epidermal growth factor receptor expressed in Chinese hamster ovary fibroblasts. Growth Factors. 1996;13(1-2):121-32.
9103388	Ilekis JV, Gariti J, Niederberger C, Scoccia B: Expression of a truncated epidermal growth factor receptor-like protein (TEGFR) in ovarian cancer. Gynecol Oncol. 1997 Apr;65(1):36-41.
9556602	Abe Y, Odaka M, Inagaki F, Lax I, Schlessinger J, Kohda D: Disulfide bond structure of human epidermal growth factor receptor. J Biol Chem. 1998 May 1;273(18):11150-7.

# Drug_Target_1_HGNC_ID:
HGNC:3236

# Drug_Target_1_HPRD_ID:
00579

# Drug_Target_1_ID:
844

# Drug_Target_1_Locus:
7p12

# Drug_Target_1_Molecular_Weight:
134279

# Drug_Target_1_Name:
Epidermal growth factor receptor

# Drug_Target_1_Number_of_Residues:
1230

# Drug_Target_1_PDB_ID:
1IVO

# Drug_Target_1_Pathway:
Cetuximab Pathway	SMP00474
Erlotinib Pathway	SMP00472
Gefitinib Pathway	SMP00473
Panitumumab Pathway	SMP00475
Trastuzumab Pathway	SMP00476

# Drug_Target_1_Pfam_Domain_Function:
PF00757	Furin-like
PF01030	Recep_L_domain
PF07714	Pkinase_Tyr

# Drug_Target_1_Protein_Sequence:
>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

# Drug_Target_1_Reaction:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate

# Drug_Target_1_Signals:
1-24

# Drug_Target_1_Specific_Function:
Isoform 2/truncated isoform may act as an antagonist

# Drug_Target_1_SwissProt_ID:
P00533

# Drug_Target_1_SwissProt_Name:
EGFR_HUMAN

# Drug_Target_1_Synonyms:
EC 2.7.10.1
Epidermal growth factor receptor precursor
Receptor tyrosine-protein kinase ErbB-1

# Drug_Target_1_Theoretical_pI:
6.67

# Drug_Target_1_Transmembrane_Regions:
646-668

# Drug_Target_2_Cellular_Location:
Cell membrane
GPI-anchor. Secreted protein. Note=Secreted after cleavage
lipid-anchor

# Drug_Target_2_Chromosome_Location:
Not Available

# Drug_Target_2_Drug_References:
16336752	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.

# Drug_Target_2_Essentiality:
Non-Essential

# Drug_Target_2_GenAtlas_ID:
FCGR3B

# Drug_Target_2_GenBank_ID_Gene:
X16863

# Drug_Target_2_GenBank_ID_Protein:
31322

# Drug_Target_2_GeneCard_ID:
FCGR3B

# Drug_Target_2_Gene_Name:
FCGR3B

# Drug_Target_2_Gene_Sequence:
>702 bp
ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT
GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGCGTGCTTGAGAAG
GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG
TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA
GTCAACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG
CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG
GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA
TATTTACAGAATGGCAAAGACAGGAAGTATTTTCATCATAATTCTGACTTCCACATTCCA
AAAGCCACACTCAAAGATAGCGGCTCCTACTTCTGCAGGGGGCTTGTTGGGAGTAAAAAT
GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA
TCATTCTCTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA
GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTTGA

# Drug_Target_2_General_Function:
Not Available

# Drug_Target_2_General_References:
10917521	Sondermann P, Huber R, Oosthuizen V, Jacob U: The 3.2-A crystal structure of the human IgG1 Fc fragment-Fc gammaRIII complex. Nature. 2000 Jul 20;406(6793):267-73.
11021536	Zhang Y, Boesen CC, Radaev S, Brooks AG, Fridman WH, Sautes-Fridman C, Sun PD: Crystal structure of the extracellular domain of a human Fc gamma RIII. Immunity. 2000 Sep;13(3):387-95.
2521732	Peltz GA, Grundy HO, Lebo RV, Yssel H, Barsh GS, Moore KW: Human Fc gamma RIII: cloning, expression, and identification of the chromosomal locus of two Fc receptors for IgG. Proc Natl Acad Sci U S A. 1989 Feb;86(3):1013-7.
2525780	Scallon BJ, Scigliano E, Freedman VH, Miedel MC, Pan YC, Unkeless JC, Kochan JP: A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms. Proc Natl Acad Sci U S A. 1989 Jul;86(13):5079-83.
2526846	Ravetch JV, Perussia B: Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions. J Exp Med. 1989 Aug 1;170(2):481-97.
2967436	Simmons D, Seed B: The Fc gamma receptor of natural killer cells is a phospholipid-linked membrane protein. Nature. 1988 Jun 9;333(6173):568-70.
7836402	Gessner JE, Grussenmeyer T, Kolanus W, Schmidt RE: The human low affinity immunoglobulin G Fc receptor III-A and III-B genes. Molecular characterization of the promoter regions. J Biol Chem. 1995 Jan 20;270(3):1350-61.
9028335	Bux J, Stein EL, Bierling P, Fromont P, Clay M, Stroncek D, Santoso S: Characterization of a new alloantigen (SH) on the human neutrophil Fc gamma receptor IIIb. Blood. 1997 Feb 1;89(3):1027-34.

# Drug_Target_2_HGNC_ID:
HGNC:3620

# Drug_Target_2_HPRD_ID:
09951

# Drug_Target_2_ID:
1102

# Drug_Target_2_Locus:
1q23

# Drug_Target_2_Molecular_Weight:
26216

# Drug_Target_2_Name:
Low affinity immunoglobulin gamma Fc region receptor III-B

# Drug_Target_2_Number_of_Residues:
236

# Drug_Target_2_PDB_ID:
1E4K

# Drug_Target_2_Pathway:
Not Available

# Drug_Target_2_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_2_Protein_Sequence:
>Low affinity immunoglobulin gamma Fc region receptor III-B precursor
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQW
FHNESLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE
EDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKN
VSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI

# Drug_Target_2_Reaction:
Not Available

# Drug_Target_2_Signals:
1-16

# Drug_Target_2_Specific_Function:
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

# Drug_Target_2_SwissProt_ID:
O75015

# Drug_Target_2_SwissProt_Name:
FCG3B_HUMAN

# Drug_Target_2_Synonyms:
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

# Drug_Target_2_Theoretical_pI:
6.71

# Drug_Target_2_Transmembrane_Regions:
None

# Drug_Target_3_Cellular_Location:
Cytoplasmic

# Drug_Target_3_Chromosome_Location:
Not Available

# Drug_Target_3_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_3_Essentiality:
Non-Essential

# Drug_Target_3_GenAtlas_ID:
C1R

# Drug_Target_3_GenBank_ID_Gene:
X04701

# Drug_Target_3_GenBank_ID_Protein:
29539

# Drug_Target_3_GeneCard_ID:
C1R

# Drug_Target_3_Gene_Name:
C1R

# Drug_Target_3_Gene_Sequence:
>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

# Drug_Target_3_General_Function:
Not Available

# Drug_Target_3_General_References:
2820791	Arlaud GJ, Van Dorsselaer A, Bell A, Mancini M, Aude C, Gagnon J: Identification of erythro-beta-hydroxyasparagine in the EGF-like domain of human C1r. FEBS Lett. 1987 Sep 28;222(1):129-34.
3021205	Leytus SP, Kurachi K, Sakariassen KS, Davie EW: Nucleotide sequence of the cDNA coding for human complement C1r. Biochemistry. 1986 Aug 26;25(17):4855-63.
3030286	Journet A, Tosi M: Cloning and sequencing of full-length cDNA encoding the precursor of human complement component C1r. Biochem J. 1986 Dec 15;240(3):783-7.
3036070	Arlaud GJ, Willis AC, Gagnon J: Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme C1r. Biochem J. 1987 Feb 1;241(3):711-20.
6303394	Arlaud GJ, Gagnon J: Complete amino acid sequence of the catalytic chain of human complement subcomponent C1-r. Biochemistry. 1983 Apr 12;22(8):1758-64.
8635594	Pelloux S, Thielens NM, Hudry-Clergeon G, Petillot Y, Filhol O, Arlaud GJ: Identification of a cryptic protein kinase CK2 phosphorylation site in human complement protease Clr, and its use to probe intramolecular interaction. FEBS Lett. 1996 May 13;386(1):15-20.
9477945	Bersch B, Hernandez JF, Marion D, Arlaud GJ: Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family. Biochemistry. 1998 Feb 3;37(5):1204-14.

# Drug_Target_3_HGNC_ID:
HGNC:1246

# Drug_Target_3_HPRD_ID:
Not Available

# Drug_Target_3_ID:
3814

# Drug_Target_3_Locus:
12p13

# Drug_Target_3_Molecular_Weight:
80174

# Drug_Target_3_Name:
Complement C1r subcomponent

# Drug_Target_3_Number_of_Residues:
716

# Drug_Target_3_PDB_ID:
1GPZ

# Drug_Target_3_Pathway:
Not Available

# Drug_Target_3_Pfam_Domain_Function:
PF00084	Sushi
PF00089	Trypsin
PF00431	CUB
PF07645	EGF_CA

# Drug_Target_3_Protein_Sequence:
>Complement C1r subcomponent
MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVF
QQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDF
SNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGY
ELQEDRHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPF
DIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKL
RYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQD
DGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSR
ESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVF
TNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRV
SVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVME
EKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAV
RDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED

# Drug_Target_3_Reaction:
Selective cleavage of Lys(or Arg)!Ile bond in complement subcomponent C1s to form C_overbar_1s_ (internal_xref(ec_num(3,4,21,42)))

# Drug_Target_3_Signals:
1-17

# Drug_Target_3_Specific_Function:
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

# Drug_Target_3_SwissProt_ID:
P00736

# Drug_Target_3_SwissProt_Name:
C1R_HUMAN

# Drug_Target_3_Synonyms:
Complement C1r subcomponent precursor
Complement component 1, r subcomponent
EC 3.4.21.41

# Drug_Target_3_Theoretical_pI:
6.24

# Drug_Target_3_Transmembrane_Regions:
None

# Drug_Target_4_Cellular_Location:
Secreted protein

# Drug_Target_4_Chromosome_Location:
Not Available

# Drug_Target_4_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_4_Essentiality:
Non-Essential

# Drug_Target_4_GenAtlas_ID:
C1QA

# Drug_Target_4_GenBank_ID_Gene:
AF135157

# Drug_Target_4_GenBank_ID_Protein:
4894854

# Drug_Target_4_GeneCard_ID:
C1QA

# Drug_Target_4_Gene_Name:
C1QA

# Drug_Target_4_Gene_Sequence:
>738 bp
ATGGAGGGTCCCCGGGGATGGCTGGTGCTCTGTGTGCTGGCCATATCGCTGGCCTCTATG
GTGACCGAGGACTTGTGCCGAGCACCAGACGGGAAGAAAGGGGAGGCAGGAAGACCTGGC
AGACGGGGGCGGCCAGGCCTCAAGGGGGAGCAAGGGGAGCCGGGGGCCCCTGGCATCCGG
ACAGGCATCCAAGGCCTTAAAGGAGACCAGGGGGAACCTGGGCCCTCTGGAAACCCCGGC
AAGGTGGGCTACCCAGGGCCCAGCGGCCCCCTCGGGGCCCGTGGCATCCCGGGAATTAAA
GGCACCAAGGGCAGCCCAGGAAACATCAAGGACCAGCCGAGGCCAGCCTTCTCCGCCATT
CGGCGGAACCCCCCAATGGGGGGCAACGTGGTCATCTTCGACACGGTCATCACCAACCAG
GAAGAACCGTACCAGAACCACTCCGGCCGATTCGTCTGCACTGTACCCGGCTACTACTAC
TTCACCTTCCAGGTGCTGTCCCAGTGGGAAATCTGCCTGTCCATCGTCTCCTCCTCAAGG
GGCCAGGTCCGACGCTCCCTGGGCTTCTGTGACACCACCAACAAGGGGCTCTTCCAGGTG
GTGTCAGGGGGCATGGTGCTTCAGCTGCAGCAGGGTGACCAGGTCTGGGTTGAAAAAGAC
CCCAAAAAGGGTCACATTTACCAGGGCTCTGAGGCCGACAGCGTCTTCAGCGGCTTCCTC
ATCTTCCCATCTGCCTGA

# Drug_Target_4_General_Function:
Not Available

# Drug_Target_4_General_References:
12960167	Gaboriaud C, Juanhuix J, Gruez A, Lacroix M, Darnault C, Pignol D, Verger D, Fontecilla-Camps JC, Arlaud GJ: The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem. 2003 Nov 21;278(47):46974-82. Epub 2003 Sep 5.
1706597	Sellar GC, Blake DJ, Reid KB: Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q. Biochem J. 1991 Mar 1;274 ( Pt 2):481-90.
486087	Reid KB: Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J. 1979 May 1;179(2):367-71.
6981411	Reid KB, Gagnon J, Frampton J: Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement. Biochem J. 1982 Jun 1;203(3):559-69.
9777412	Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94.

# Drug_Target_4_HGNC_ID:
HGNC:1241

# Drug_Target_4_HPRD_ID:
Not Available

# Drug_Target_4_ID:
3815

# Drug_Target_4_Locus:
1p36.12

# Drug_Target_4_Molecular_Weight:
26017

# Drug_Target_4_Name:
Complement C1q subcomponent subunit A

# Drug_Target_4_Number_of_Residues:
249

# Drug_Target_4_PDB_ID:
1PK6

# Drug_Target_4_Pathway:
Not Available

# Drug_Target_4_Pfam_Domain_Function:
PF00386	C1q
PF01391	Collagen

# Drug_Target_4_Protein_Sequence:
>Complement C1q subcomponent subunit A
MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIR
TGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAI
RRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSR
GQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFL
IFPSA

# Drug_Target_4_Reaction:
Not Available

# Drug_Target_4_Signals:
1-22

# Drug_Target_4_Specific_Function:
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

# Drug_Target_4_SwissProt_ID:
P02745

# Drug_Target_4_SwissProt_Name:
C1QA_HUMAN

# Drug_Target_4_Synonyms:
Complement C1q subcomponent subunit A precursor

# Drug_Target_4_Theoretical_pI:
9.45

# Drug_Target_4_Transmembrane_Regions:
None

# Drug_Target_5_Cellular_Location:
Secreted protein

# Drug_Target_5_Chromosome_Location:
Not Available

# Drug_Target_5_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_5_Essentiality:
Non-Essential

# Drug_Target_5_GenAtlas_ID:
C1QB

# Drug_Target_5_GenBank_ID_Gene:
X03084

# Drug_Target_5_GenBank_ID_Protein:
573114

# Drug_Target_5_GeneCard_ID:
C1QB

# Drug_Target_5_Gene_Name:
C1QB

# Drug_Target_5_Gene_Sequence:
>688 bp
CCAGGCCCAGCTCAGCTGCACCGGGCCCCCAGCCATCCCTGGCATCCCGGGTATCCCTGG
GACACCTGGCCCCGATGGCCAACCTGGGACCCCAGGGATAAAAGGAGAGAAAGGGCTTCC
AGGGCTGGCTGGAGACCATGGTGAGTTCGGAGAGAAGGGAGACCCAGGGATTCCTGGGAA
TCCAGGAAAAGTCGGCCCCAAGGGCCCCATGGGCCCTAAAGGTGGCCCAGGGGCCCCTGG
AGCCCCAGGCCCCAAAGGTGAATCGGGAGACTACAAGGCCACCCAGAAAATCGCCTTCTC
TGCCACAAGAACCATCAACGTCCCCCTGCGCCGGGACCAGACCATCCGCTTCGACCACGT
GATCACCAACATGAACAACAATTATGAGCCCCGCAGTGGCAAGTTCACCTGCAAGGTGCC
CGGTCTCTACTACTTCACCTACCACGCCAGCTCTCGAGGGAACCTGTGCGTGAACCTCAT
GCGTGGCCGGGAGCGTGCACAGAAGGTGGTCACCTTCTGTGACTATGCCTACAACACCTT
CCAGGTCACCACCGGTGGCATGGTCCTCAAGCTGGAGCAGGGGGAGAACGTCTTCCTGCA
GGCCACCGACAAGAACTCACTACTGGGCATGGAGGGTGCCAACAGCATCTTTTCCGGGTT
CCTGCTCTTTCCAGATATGGAGGCCTGA

# Drug_Target_5_General_Function:
Not Available

# Drug_Target_5_General_References:
12960167	Gaboriaud C, Juanhuix J, Gruez A, Lacroix M, Darnault C, Pignol D, Verger D, Fontecilla-Camps JC, Arlaud GJ: The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem. 2003 Nov 21;278(47):46974-82. Epub 2003 Sep 5.
3000358	Reid KB: Molecular cloning and characterization of the complementary DNA and gene coding for the B-chain of subcomponent C1q of the human complement system. Biochem J. 1985 Nov 1;231(3):729-35.
486087	Reid KB: Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J. 1979 May 1;179(2):367-71.
6208566	Reid KB, Bentley DR, Wood KJ: Cloning and characterization of the complementary DNA for the B chain of normal human serum C1q. Philos Trans R Soc Lond B Biol Sci. 1984 Sep 6;306(1129):345-54.
6981411	Reid KB, Gagnon J, Frampton J: Completion of the amino acid sequences of the A and B chains of subcomponent C1q of the first component of human complement. Biochem J. 1982 Jun 1;203(3):559-69.
708376	Reid KB, Thompson EO: Amino acid sequence of the N-terminal 108 amino acid residues of the B chain of subcomponent C1q of the first component of human complement. Biochem J. 1978 Sep 1;173(3):863-8.
9777412	Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94.

# Drug_Target_5_HGNC_ID:
HGNC:1242

# Drug_Target_5_HPRD_ID:
Not Available

# Drug_Target_5_ID:
3816

# Drug_Target_5_Locus:
1p36.12

# Drug_Target_5_Molecular_Weight:
26460

# Drug_Target_5_Name:
Complement C1q subcomponent subunit B

# Drug_Target_5_Number_of_Residues:
255

# Drug_Target_5_PDB_ID:
1PK6

# Drug_Target_5_Pathway:
Not Available

# Drug_Target_5_Pfam_Domain_Function:
PF00386	C1q
PF01391	Collagen

# Drug_Target_5_Protein_Sequence:
>Complement C1q subcomponent subunit B
MKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEK
GLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKI
AFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCV
NLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIF
SGFLLFPDMEA

# Drug_Target_5_Reaction:
Not Available

# Drug_Target_5_Signals:
1-25

# Drug_Target_5_Specific_Function:
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

# Drug_Target_5_SwissProt_ID:
P02746

# Drug_Target_5_SwissProt_Name:
C1QB_HUMAN

# Drug_Target_5_Synonyms:
Complement C1q subcomponent subunit B precursor

# Drug_Target_5_Theoretical_pI:
8.87

# Drug_Target_5_Transmembrane_Regions:
None

# Drug_Target_6_Cellular_Location:
Secreted protein

# Drug_Target_6_Chromosome_Location:
Not Available

# Drug_Target_6_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_6_Essentiality:
Non-Essential

# Drug_Target_6_GenAtlas_ID:
C1QC

# Drug_Target_6_GenBank_ID_Gene:
AF087892

# Drug_Target_6_GenBank_ID_Protein:
33150626

# Drug_Target_6_GeneCard_ID:
C1QC

# Drug_Target_6_Gene_Name:
C1QC

# Drug_Target_6_Gene_Sequence:
>738 bp
ATGGACGTGGGGCCCAGCTCCCTGCCCCACCTTGGGCTGAAGCTGCTGCTGCTCCTGCTG
CTGCTGCCCCTCAGGGCCAAAGCCAACACAGGCTGCTACGGGATCCCAGGGATGCCCGGC
CTGCCCGGGGCACCAGGGAAGGATGGGTACGACGGACTGCCGGGGCCCAAGGGGGAGCCA
GGAATCCCAGCCATTCCCGGGATCCGAGGACCCAAAGGGCAGAAGGGAGAACCCGGCTTA
CCCGGCCATCCTGGGAAAAATGGCCCCATGGGACCCCCTGGGATGCCAGGGGTGCCCGGC
CCCATGGGATTCCCTGGAGAGCCAGGTGAGGAGGGCAGATACAAGCAGAAATTCCAGTCA
GTGTTCACGGTCACTCGGCAGACCCACCAGCCCCCTGCACCCAACAGCCTGATCAGATTC
AACGCGGTCCTCACCAACCCGCAGGAGGATTATGACACGAGCACTGGCAAGTTCACCTGC
AAAGTCCCCGGCCTCTACTACTTTGTCTACCACGCGTCGCATACAGCCAACCTGTGCGTG
CTGCTGTACCGCAGCGGCGTCAAAGTGGTCACCTTCTGTGGCCACACGTCCAAAACCAAT
CAGGTCAACTCGGGCGGTGTGCTGCTGAGGTTGCAGGTGGGCGAGGAGGTGTGGCTGGCT
GTCAATGACTACTACGACATGGTGGGCATCCAGGGCTCTGACAGCGTCTTCTCCGGCTTC
CTGCTCTTCCCCGACTAG

# Drug_Target_6_General_Function:
Not Available

# Drug_Target_6_General_References:
12960167	Gaboriaud C, Juanhuix J, Gruez A, Lacroix M, Darnault C, Pignol D, Verger D, Fontecilla-Camps JC, Arlaud GJ: The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem. 2003 Nov 21;278(47):46974-82. Epub 2003 Sep 5.
1706597	Sellar GC, Blake DJ, Reid KB: Characterization and organization of the genes encoding the A-, B- and C-chains of human complement subcomponent C1q. The complete derived amino acid sequence of human C1q. Biochem J. 1991 Mar 1;274 ( Pt 2):481-90.
486087	Reid KB: Complete amino acid sequences of the three collagen-like regions present in subcomponent C1q of the first component of human complement. Biochem J. 1979 May 1;179(2):367-71.
9777412	Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94.

# Drug_Target_6_HGNC_ID:
HGNC:1245

# Drug_Target_6_HPRD_ID:
Not Available

# Drug_Target_6_ID:
3817

# Drug_Target_6_Locus:
1p36.11

# Drug_Target_6_Molecular_Weight:
25774

# Drug_Target_6_Name:
Complement C1q subcomponent subunit C

# Drug_Target_6_Number_of_Residues:
249

# Drug_Target_6_PDB_ID:
1PK6

# Drug_Target_6_Pathway:
Not Available

# Drug_Target_6_Pfam_Domain_Function:
PF00386	C1q
PF01391	Collagen

# Drug_Target_6_Protein_Sequence:
>Complement C1q subcomponent subunit C
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEP
GIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQS
VFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCV
LLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGF
LLFPD

# Drug_Target_6_Reaction:
Not Available

# Drug_Target_6_Signals:
1-28

# Drug_Target_6_Specific_Function:
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

# Drug_Target_6_SwissProt_ID:
P02747

# Drug_Target_6_SwissProt_Name:
C1QC_HUMAN

# Drug_Target_6_Synonyms:
Complement C1q subcomponent subunit C precursor

# Drug_Target_6_Theoretical_pI:
8.58

# Drug_Target_6_Transmembrane_Regions:
None

# Drug_Target_7_Cellular_Location:
Cell membrane

# Drug_Target_7_Chromosome_Location:
Not Available

# Drug_Target_7_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.
17704420	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.

# Drug_Target_7_Essentiality:
Non-Essential

# Drug_Target_7_GenAtlas_ID:
FCGR3A

# Drug_Target_7_GenBank_ID_Gene:
X52645

# Drug_Target_7_GenBank_ID_Protein:
31324

# Drug_Target_7_GeneCard_ID:
FCGR3A

# Drug_Target_7_Gene_Name:
FCGR3A

# Drug_Target_7_Gene_Sequence:
>765 bp
ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT
GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGGGTGCTCGAGAAG
GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG
TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA
GTCGACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG
CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG
GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA
TATTTACAGAATGGCAAAGGCAGGAAGTATTTTCATCATAATTCTGACTTCTACATTCCA
AAAGCCACACTCAAAGACAGCGGCTCCTACTTCTGCAGGGGGCTTTTTGGGAGTAAAAAT
GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA
TCATTCTTTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA
GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTCGAAGCTCAACAAGAGACTGG
AAGGACCATAAATTTAAATGGAGAAAGGACCCTCAAGACAAATGA

# Drug_Target_7_General_Function:
Not Available

# Drug_Target_7_General_References:
2526846	Ravetch JV, Perussia B: Alternative membrane forms of Fc gamma RIII(CD16) on human natural killer cells and neutrophils. Cell type-specific expression of two genes that differ in single nucleotide substitutions. J Exp Med. 1989 Aug 1;170(2):481-97.
7836402	Gessner JE, Grussenmeyer T, Kolanus W, Schmidt RE: The human low affinity immunoglobulin G Fc receptor III-A and III-B genes. Molecular characterization of the promoter regions. J Biol Chem. 1995 Jan 20;270(3):1350-61.
8609432	de Haas M, Koene HR, Kleijer M, de Vries E, Simsek S, van Tol MJ, Roos D, von dem Borne AE: A triallelic Fc gamma receptor type IIIA polymorphism influences the binding of human IgG by NK cell Fc gamma RIIIa. J Immunol. 1996 Apr 15;156(8):3948-55.
9242542	Koene HR, Kleijer M, Algra J, Roos D, von dem Borne AE, de Haas M: Fc gammaRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell Fc gammaRIIIa, independently of the Fc gammaRIIIa-48L/R/H phenotype. Blood. 1997 Aug 1;90(3):1109-14.
9276722	Wu J, Edberg JC, Redecha PB, Bansal V, Guyre PM, Coleman K, Salmon JE, Kimberly RP: A novel polymorphism of FcgammaRIIIa (CD16) alters receptor function and predisposes to autoimmune disease. J Clin Invest. 1997 Sep 1;100(5):1059-70.

# Drug_Target_7_HGNC_ID:
HGNC:3619

# Drug_Target_7_HPRD_ID:
Not Available

# Drug_Target_7_ID:
3818

# Drug_Target_7_Locus:
1q23

# Drug_Target_7_Molecular_Weight:
29089

# Drug_Target_7_Name:
Low affinity immunoglobulin gamma Fc region receptor III-A

# Drug_Target_7_Number_of_Residues:
258

# Drug_Target_7_PDB_ID:
1E4K

# Drug_Target_7_Pathway:
Not Available

# Drug_Target_7_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_7_Protein_Sequence:
>Low affinity immunoglobulin gamma Fc region receptor III-A
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQW
FHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE
EDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKN
VSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDW
KDHKFKWRKDPQDK

# Drug_Target_7_Reaction:
Not Available

# Drug_Target_7_Signals:
1-16

# Drug_Target_7_Specific_Function:
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

# Drug_Target_7_SwissProt_ID:
P08637

# Drug_Target_7_SwissProt_Name:
FCG3A_HUMAN

# Drug_Target_7_Synonyms:
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

# Drug_Target_7_Theoretical_pI:
8.21

# Drug_Target_7_Transmembrane_Regions:
209-229

# Drug_Target_8_Cellular_Location:
Cytoplasmic

# Drug_Target_8_Chromosome_Location:
Not Available

# Drug_Target_8_Drug_References:
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.

# Drug_Target_8_Essentiality:
Non-Essential

# Drug_Target_8_GenAtlas_ID:
C1S

# Drug_Target_8_GenBank_ID_Gene:
X06596

# Drug_Target_8_GenBank_ID_Protein:
763110

# Drug_Target_8_GeneCard_ID:
C1S

# Drug_Target_8_Gene_Name:
C1S

# Drug_Target_8_Gene_Sequence:
>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

# Drug_Target_8_General_Function:
Involved in calcium ion binding

# Drug_Target_8_General_References:
11390518	Dragon-Durey MA, Quartier P, Fremeaux-Bacchi V, Blouin J, de Barace C, Prieur AM, Weiss L, Fridman WH: Molecular basis of a selective C1s deficiency associated with early onset multiple autoimmune diseases. J Immunol. 2001 Jun 15;166(12):7612-6.
1854725	Illy C, Thielens NM, Gagnon J, Arlaud GJ: Effect of lactoperoxidase-catalyzed iodination on the Ca(2+)-dependent interactions of human C1s. Location of the iodination sites. Biochemistry. 1991 Jul 23;30(29):7135-41.
2007122	Hess D, Schaller J, Rickli EE: Identification of the disulfide bonds of human complement C1s. Biochemistry. 1991 Mar 19;30(11):2827-33.
2459702	Kusumoto H, Hirosawa S, Salier JP, Hagen FS, Kurachi K: Human genes for complement components C1r and C1s in a close tail-to-tail arrangement. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7307-11.
2553984	Tosi M, Duponchel C, Meo T, Couture-Tosi E: Complement genes C1r and C1s feature an intronless serine protease domain closely related to haptoglobin. J Mol Biol. 1989 Aug 20;208(4):709-14.
2831944	Tosi M, Duponchel C, Meo T, Julier C: Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr. Biochemistry. 1987 Dec 29;26(26):8516-24.
3007145	Spycher SE, Nick H, Rickli EE: Human complement component C1s. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation. Eur J Biochem. 1986 Apr 1;156(1):49-57.
3500856	Mackinnon CM, Carter PE, Smyth SJ, Dunbar B, Fothergill JE: Molecular cloning of cDNA for human complement component C1s. The complete amino acid sequence. Eur J Biochem. 1987 Dec 15;169(3):547-53.
6362661	Carter PE, Dunbar B, Fothergill JE: The serine proteinase chain of human complement component C1s. Cyanogen bromide cleavage and N-terminal sequences of the fragments. Biochem J. 1983 Dec 1;215(3):565-71.
7779774	Rossi V, Gaboriaud C, Lacroix M, Ulrich J, Fontecilla-Camps JC, Gagnon J, Arlaud GJ: Structure of the catalytic region of human complement protease C1s: study by chemical cross-linking and three-dimensional homology modeling. Biochemistry. 1995 Jun 6;34(22):7311-21.
9794427	Endo Y, Takahashi M, Nakao M, Saiga H, Sekine H, Matsushita M, Nonaka M, Fujita T: Two lineages of mannose-binding lectin-associated serine protease (MASP) in vertebrates. J Immunol. 1998 Nov 1;161(9):4924-30.

# Drug_Target_8_HGNC_ID:
HGNC:1247

# Drug_Target_8_HPRD_ID:
00397

# Drug_Target_8_ID:
2782

# Drug_Target_8_Locus:
12p13

# Drug_Target_8_Molecular_Weight:
76685

# Drug_Target_8_Name:
Complement C1s subcomponent

# Drug_Target_8_Number_of_Residues:
699

# Drug_Target_8_PDB_ID:
1ELV

# Drug_Target_8_Pathway:
Not Available

# Drug_Target_8_Pfam_Domain_Function:
PF00008	EGF
PF00084	Sushi
PF00089	Trypsin
PF00431	CUB

# Drug_Target_8_Protein_Sequence:
>Complement C1s subcomponent precursor
MWCIVLFSLLAWVYAEPTMYGEILSPNYPQAYPSEVEKSWDIEVPEGYGIHLYFTHLDIE
LSENCAYDSVQIISGDTEEGRLCGQRSSNNPHSPIVEEFQVPYNKLQVIFKSDFSNEERF
TGFAAYYVATDINECTDFVDVPCSHFCNNFIGGYFCSCPPEYFLHDDMKNCGVNCSGDVF
TALIGEIASPNYPKPYPENSRCEYQIRLEKGFQVVVTLRREDFDVEAADSAGNCLDSLVF
VAGDRQFGPYCGHGFPGPLNIETKSNALDIIFQTDLTGQKKGWKLRYHGDPMPCPKEDTP
NSVWEPAKAKYVFRDVVQITCLDGFEVVEGRVGATSFYSTCQSNGKWSNSKLKCQPVDCG
IPESIENGKVEDPESTLFGSVIRYTCEEPYYYMENGGGGEYHCAGNGSWVNEVLGPELPK
CVPVCGVPREPFEEKQRIIGGSDADIKNFPWQVFFDNPWAGGALINEYWVLTAAHVVEGN
REPTMYVGSTSVQTSRLAKSKMLTPEHVFIHPGWKLLEVPEGRTNFDNDIALVRLKDPVK
MGPTVSPICLPGTSSDYNLMDGDLGLISGWGRTEKRDRAVRLKAARLPVAPLRKCKEVKV
EKPTADAEAYVFTPNMICAGGEKGMDSCKGDSGGAFAVQDPNDKTKFYAAGLVSWGPQCG
TYGLYTRVKNYVDWIMKTMQENSTPRED

# Drug_Target_8_Reaction:
Cleavage of Arg!Ala bond in complement component C4 to form C4a and C4b, and Lys(or Arg)!Lys bond in complement component C2 to form C2a and C2b: the "classical" pathway C3 convertase

# Drug_Target_8_Signals:
1-15

# Drug_Target_8_Specific_Function:
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

# Drug_Target_8_SwissProt_ID:
P09871

# Drug_Target_8_SwissProt_Name:
C1S_HUMAN

# Drug_Target_8_Synonyms:
C1 esterase
Complement C1s subcomponent precursor
EC 3.4.21.42

# Drug_Target_8_Theoretical_pI:
4.59

# Drug_Target_8_Transmembrane_Regions:
None

# Drug_Target_9_Cellular_Location:
Membrane
single-pass type I membrane protein

# Drug_Target_9_Chromosome_Location:
Not Available

# Drug_Target_9_Drug_References:
7547242	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.

# Drug_Target_9_Essentiality:
Non-Essential

# Drug_Target_9_GenAtlas_ID:
FCGR1A

# Drug_Target_9_GenBank_ID_Gene:
X14356

# Drug_Target_9_GenBank_ID_Protein:
31332

# Drug_Target_9_GeneCard_ID:
FCGR1A

# Drug_Target_9_Gene_Name:
FCGR1A

# Drug_Target_9_Gene_Sequence:
>1125 bp
ATGTGGTTCTTGACAACTCTGCTCCTTTGGGTTCCAGTTGATGGGCAAGTGGACACCACA
AAGGCAGTGATCTCTTTGCAGCCTCCATGGGTCAGCGTGTTCCAAGAGGAAACCGTAACC
TTGCACTGTGAGGTGCTCCATCTGCCTGGGAGCAGCTCTACACAGTGGTTTCTCAATGGC
ACAGCCACTCAGACCTCGACCCCCAGCTACAGAATCACCTCTGCCAGTGTCAATGACAGT
GGTGAATACAGGTGCCAGAGAGGTCTCTCAGGGCGAAGTGACCCCATACAGCTGGAAATC
CACAGAGGCTGGCTACTACTGCAGGTCTCCAGCAGAGTCTTCACGGAAGGAGAACCTCTG
GCCTTGAGGTGTCATGCGTGGAAGGATAAGCTGGTGTACAATGTGCTTTACTATCGAAAT
GGCAAAGCCTTTAAGTTTTTCCACTGGAATTCTAACCTCACCATTCTGAAAACCAACATA
AGTCACAATGGCACCTACCATTGCTCAGGCATGGGAAAGCATCGCTACACATCAGCAGGA
ATATCTGTCACTGTGAAAGAGCTATTTCCAGCTCCAGTGCTGAATGCATCTGTGACATCC
CCACTCCTGGAGGGGAATCTGGTCACCCTGAGCTGTGAAACAAAGTTGCTCTTGCAGAGG
CCTGGTTTGCAGCTTTACTTCTCCTTCTACATGGGCAGCAAGACCCTGCGAGGCAGGAAC
ACATCCTCTGAATACCAAATACTAACTGCTAGAAGAGAAGACTCTGGGTTATACTGGTGC
GAGGCTGCCACAGAGGATGGAAATGTCCTTAAGCGCAGCCCTGAGTTGGAGCTTCAAGTG
CTTGGCCTCCAGTTACCAACTCCTGTCTGGTTTCATGTCCTTTTCTATCTGGCAGTGGGA
ATAATGTTTTTAGTGAACACTGTTCTCTGGGTGACAATACGTAAAGAACTGAAAAGAAAG
AAAAAGTGGGATTTAGAAATCTCTTTGGATTCTGGTCATGAGAAGAAGGTAACTTCCAGC
CTTCAAGAAGACAGACATTTAGAAGAAGAGCTGAAATGTCAGGAACAAAAAGAAGAACAG
CTGCAGGAAGGGGTGCACCGGAAGGAGCCCCAGGGGGCCACGTAG

# Drug_Target_9_General_Function:
Involved in receptor signaling protein activity

# Drug_Target_9_General_References:
1379234	Ernst LK, van de Winkel JG, Chiu IM, Anderson CL: Three genes for the human high affinity Fc receptor for IgG (Fc gamma RI) encode four distinct transcription products. J Biol Chem. 1992 Aug 5;267(22):15692-700.
1402657	Benech PD, Sastry K, Iyer RR, Eichbaum QG, Raveh DP, Ezekowitz RA: Definition of interferon gamma-response elements in a novel human Fc gamma receptor gene (Fc gamma RIb) and characterization of the gene structure. J Exp Med. 1992 Oct 1;176(4):1115-23.
1430234	Porges AJ, Redecha PB, Doebele R, Pan LC, Salmon JE, Kimberly RP: Novel Fc gamma receptor I family gene products in human mononuclear cells. J Clin Invest. 1992 Nov;90(5):2102-9.
2911749	Allen JM, Seed B: Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science. 1989 Jan 20;243(4889):378-81.
2974947	Allen JM, Seed B: Nucleotide sequence of three cDNAs for the human high affinity Fc receptor (FcRI). Nucleic Acids Res. 1988 Dec 23;16(24):11824.

# Drug_Target_9_HGNC_ID:
HGNC:3613

# Drug_Target_9_HPRD_ID:
00904

# Drug_Target_9_ID:
784

# Drug_Target_9_Locus:
1q21.2-q21.3

# Drug_Target_9_Molecular_Weight:
42632

# Drug_Target_9_Name:
High affinity immunoglobulin gamma Fc receptor I

# Drug_Target_9_Number_of_Residues:
380

# Drug_Target_9_PDB_ID:
Not Available

# Drug_Target_9_Pathway:
Not Available

# Drug_Target_9_Pfam_Domain_Function:
PF00047	ig

# Drug_Target_9_Protein_Sequence:
>High affinity immunoglobulin gamma Fc receptor I precursor
MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNG
TATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPL
ALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAG
ISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRN
TSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVG
IMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQ
LQEGVHRKEPQGAT

# Drug_Target_9_Reaction:
Not Available

# Drug_Target_9_Signals:
1-15

# Drug_Target_9_Specific_Function:
Binds to the Fc region of immunoglobulins gamma. High affinity receptor

# Drug_Target_9_SwissProt_ID:
P12314

# Drug_Target_9_SwissProt_Name:
FCGR1_HUMAN

# Drug_Target_9_Synonyms:
CD64 antigen
Fc-gamma RI
FcRI
High affinity immunoglobulin gamma Fc receptor I precursor
IgG Fc receptor I

# Drug_Target_9_Theoretical_pI:
8.08

# Drug_Target_9_Transmembrane_Regions:
293-313

#END_DRUGCARD DB00002
#BEGIN_DRUGCARD DB00003

# AHFS_Codes:
44:00

# ATC_Codes:
R05CB13

# Absorption:
Systemic absorption undetectable following administration by inhalation.

# Biotransformation:
Not Available

# Brand_Mixtures:
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)

# Brand_Names:
Pulmozyme
Viscozyme

# CAS_Registry_Number:
9003-98-9

# ChEBI_ID:
Not Available

# Chemical_Formula:
C1321H1999N339O396S9

# Chemical_IUPAC_Name:
Not Available

# Chemical_Structure:
>DB00003 sequence
LKIAAFNIQTFGETKMSNATLVSYIVQILSRYDIALVQEVRDSHLTAVGKLLDNLNQDAP
DTYHYVVSEPLGRNSYKERYLFVYRPDQVSAVDSYYYDDGCEPCGNDTFNREPAIVRFFS
RFTEVREFAIVPLHAAPGDAVAEIDALYDVYLDVQEKWGLEDVMLMGDFNAGCSYVRPSQ
WSSIRLWTSPTFQWLIPDSADTTATPTHCAYDRIVVAGMLLRGAVVPDSALPFNFQAAYG
LSDQLAQAISDHYPVEVMLK

# Creation_Date:
2005-06-13 07:24:05 -0600

# DPD_Drug_ID_Number:
02046733

# Description:
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.

# Dosage_Forms:
Solution	Respiratory (inhalation)

# Drug_Category:
Enzyme

# Drug_Interactions:
Not Available

# Drug_Reference:
19255515	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.
20238314	Jones AP, Wallis C: Dornase alfa for cystic fibrosis. Cochrane Database Syst Rev. 2010 Mar 17;3:CD001127.
8792953	Cramer GW, Bosso JA: The role of dornase alfa in the treatment of cystic fibrosis. Ann Pharmacother. 1996 Jun;30(6):656-61.

# Drug_Type:
Approved
Biotech

# Experimental_Caco2_Permeability:
Not Available

# Experimental_LogP_Hydrophobicity:
-0.083

# Experimental_Logs:
Not Available

# Experimental_Water_Solubility:
Not Available

# Food_Interactions:
Not Available

# GenBank_ID:
M55983

# Generic_Name:
Dornase Alfa

# HET_ID:
Not Available

# Half_Life:
Not Available

# InChI_Identifier:
Not Available

# InChI_Key:
Not Available

# Indication:
Used as adjunct therapy in the treatment of cystic fibrosis.

# KEGG_Compound_ID:
Not Available

# KEGG_Drug_ID:
Not Available

# LIMS_Drug_ID:
3

# Mechanism_Of_Action:
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.

# Melting_Point:
67 oC (Chan, H.K. et al., Pharm Res. 13:756-761 (1996))

# Molecular_Weight_Avg:
29253.9000

# Molecular_Weight_Mono:
Not Available

# Organisms_Affected:
Humans and other mammals

# PDB_Experimental_ID:
3DNI

# PDB_Homology_ID:
Not Available

# PDRhealth_Link:
Not Available

# Pathways:
Not Available

# PharmGKB_ID:
PA10318

# Pharmacology:
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.

# Predicted_LogP_Hydrophobicity:
Not Available

# Predicted_LogS:
Not Available

# Predicted_Water_Solubility:
Not Available

# Primary_Accession_No:
DB00003

# Protein_Binding:
Not Available

# PubChem_Compound_ID:
Not Available

# PubChem_Substance_ID:
Not Available

# RxList_Link:
http://www.rxlist.com/cgi/generic/pulmozyme.htm

# Secondary_Accession_No:
BIOD00001
BTD00001

# Smiles_String_canonical:
Not Available

# Smiles_String_isomeric:
Not Available

# State:
liquid

# Structure:
0

# SwissProt_ID:
P24855

# SwissProt_Name:
DNAS1_HUMAN

# Synonyms:
DNase
DNase I
Deoxyribonuclease I
Deoxyribonuclease-1 precursor
rhDNase

# Synthesis_Reference:
Not Available

# Toxicity:
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.

# Update_Date:
2010-09-29 14:34:47 -0600

# Wikipedia_Link:
http://en.wikipedia.org/wiki/Dornase_alfa

# pKa_Isoelectric_Point:
4.58

# Drug_Target_1_Cellular_Location:
Nucleus and mitochondria

# Drug_Target_1_Chromosome_Location:
Not Available

# Drug_Target_1_Drug_References:
8792953	Cramer GW, Bosso JA: The role of dornase alfa in the treatment of cystic fibrosis. Ann Pharmacother. 1996 Jun;30(6):656-61.

# Drug_Target_1_Essentiality:
Non-Essential

# Drug_Target_1_GenAtlas_ID:
Not Available

# Drug_Target_1_GenBank_ID_Gene:
Not Available

# Drug_Target_1_GenBank_ID_Protein:
Not Available

# Drug_Target_1_GeneCard_ID:
Not Available

# Drug_Target_1_Gene_Name:
Not Available

# Drug_Target_1_Gene_Sequence:
>Example: Dickerson dodecamer
CGCGAATTCGCG

# Drug_Target_1_General_Function:
Biological information storage and information transfer

# Drug_Target_1_General_References:
1234	Nadeau D, Marchand C: Change in the kinetics of sulphacetamide tissue distribution in Walker tumor-bearing rats. Drug Metab Dispos. 1975 Nov-Dec;3(6):565-76.

# Drug_Target_1_HGNC_ID:
Not Available

# Drug_Target_1_HPRD_ID:
Not Available

# Drug_Target_1_ID:
874

# Drug_Target_1_Locus:
All loci

# Drug_Target_1_Molecular_Weight:
7656 (double strand)

# Drug_Target_1_Name:
DNA

# Drug_Target_1_Number_of_Residues:
0

# Drug_Target_1_PDB_ID:
1BNA

# Drug_Target_1_Pathway:
Not Available

# Drug_Target_1_Pfam_Domain_Function:
Not Available

# Drug_Target_1_Protein_Sequence:
Not Available

# Drug_Target_1_Reaction:
DNA + DNA polymerase + nNTP = 2 DNA + nNDP; DNA + RNA polymerase + NTP = mRNA + nNDP

# Drug_Target_1_Signals:
None

# Drug_Target_1_Specific_Function:
DNA is the molecule of heredity, as it is responsible for the genetic propagation of most inherited traits. It is a polynucleic acid that carries genetic information on cell growth, division, and function. DNA consists of two long strands of nucleotides twisted into a double helix and held together by hydrogen bonds. The sequence of nucleotides determines hereditary characteristics. Each strand serves as the template for subsequent DNA replication and as a template for mRNA production, leading to protein synthesis via ribosomes.

# Drug_Target_1_SwissProt_ID:
Not Available

# Drug_Target_1_SwissProt_Name:
Not Available

# Drug_Target_1_Synonyms:
Deoxyribonucleic acid

# Drug_Target_1_Theoretical_pI:
Not Available

# Drug_Target_1_Transmembrane_Regions:
None

#END_DRUGCARD DB00003
#BEGIN_DRUGCARD DB00004

# AHFS_Codes:
Not Available

# ATC_Codes:
L01XX29

# Absorption:
Not Available

# Biotransformation:
Not Available

# Brand_Mixtures:
Not Available

# Brand_Names:
Ontak

# CAS_Registry_Number:
173146-27-5

# ChEBI_ID:
Not Available

# Chemical_Formula:
C2560H4042N678O799S17

# Chemical_IUPAC_Name:
Not Available

# Chemical_Structure:
>DB00004 sequence
MGADDVVDSSKSFVMENFSSYHGTKPGYVDSIQKGIQKPKSGTQGNYDDDWKGFYSTDNK
YDAAGYSVDNENPLSGKAGGVVKVTYPGLTKVLALKVDNAETIKKELGLSLTEPLMEQVG
TEEFIKRFGDGASRVVLSLPFAEGSSSVEYINNWEQAKALSVELEINFETRGKRGQDAMY
EYMAQACAGNRVRRSVGSSLSCINLDWDVIRDKTKTKIESLKEHGPIKNKMSESPNKTVS
EEKAKQYLEEFHQTALEHPELSELKTVTGTNPVFAGANYAAWAVNVAQVIDSETADNLEK
TTAALSILPGIGSVMGIADGAVHHNTEEIVAQSIALSSLMVAQAIPLVGELVDIGFAAYN
FVESIINLFQVVHNSYNRPAYSPGHKTHAPTSSSTKKTQLQLEHLLLDLQMILNGINNYK
NPKLTRMLTFKFYMPKKATELKHLQCLEEELKPLEEVLNLAQSKNFHLRPRDLISNINVI
VLELKGSETTFMCEYADETATIVEFLNRWITFCQSIISTLT

# Creation_Date:
2005-06-13 07:24:05 -0600

# DPD_Drug_ID_Number:
Not Available

# Description:
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.

# Dosage_Forms:
Solution	Intravenous

# Drug_Category:
Antineoplastic Agents

# Drug_Interactions:
Not Available

# Drug_Reference:
17187516	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.
17454642	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.

# Drug_Type:
Approved
Biotech
Investigational

# Experimental_Caco2_Permeability:
Not Available

# Experimental_LogP_Hydrophobicity:
-0.301

# Experimental_Logs:
Not Available

# Experimental_Water_Solubility:
Not Available

# Food_Interactions:
Not Available

# GenBank_ID:
V01536

# Generic_Name:
Denileukin diftitox

# HET_ID:
Not Available

# Half_Life:
70-80 min

# InChI_Identifier:
Not Available

# InChI_Key:
Not Available

# Indication:
For treatment of cutaneous T-cell lymphoma

# KEGG_Compound_ID:
Not Available

# KEGG_Drug_ID:
Not Available

# LIMS_Drug_ID:
4

# Mechanism_Of_Action:
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.

# Melting_Point:
Not Available

# Molecular_Weight_Avg:
57647.3000

# Molecular_Weight_Mono:
Not Available

# Organisms_Affected:
Humans and other mammals

# PDB_Experimental_ID:
1F0L
1M47
1SGK

# PDB_Homology_ID:
Not Available

# PDRhealth_Link:
Not Available

# Pathways:
Not Available

# PharmGKB_ID:
PA10317

# Pharmacology:
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.

# Predicted_LogP_Hydrophobicity:
Not Available

# Predicted_LogS:
Not Available

# Predicted_Water_Solubility:
Not Available

# Primary_Accession_No:
DB00004

# Protein_Binding:
Not Available

# PubChem_Compound_ID:
Not Available

# PubChem_Substance_ID:
Not Available

# RxList_Link:
http://www.rxlist.com/cgi/generic2/denileukin.htm

# Secondary_Accession_No:
BIOD00084
BTD00084

# Smiles_String_canonical:
Not Available

# Smiles_String_isomeric:
Not Available

# State:
liquid

# Structure:
0

# SwissProt_ID:
P00587

# SwissProt_Name:
DTX_COROM

# Synonyms:
DT
Diphtheria toxin precursor
NAD(+--diphthamide ADP- ribosyltransferase)
denileukin diftitox

# Synthesis_Reference:
Not Available

# Toxicity:
Not Available

# Update_Date:
2010-09-29 14:34:47 -0600

# Wikipedia_Link:
http://en.wikipedia.org/wiki/Denileukin_diftitox

# pKa_Isoelectric_Point:
5.45

# Drug_Target_1_Cellular_Location:
Membrane
single-pass type I membrane protein

# Drug_Target_1_Chromosome_Location:
Not Available

# Drug_Target_1_Drug_References:
11752352	Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5.
17016423	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.
17139284	Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6.
17187516	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.
18684057	Duvic M, Talpur R: Optimizing denileukin diftitox (Ontak) therapy. Future Oncol. 2008 Aug;4(4):457-69.
2786749	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.
3124610	Murphy JR, Kelley VE, Strom TB: Interleukin 2 toxin: a step toward selective immunomodulation. Am J Kidney Dis. 1988 Feb;11(2):159-62.

# Drug_Target_1_Essentiality:
Non-Essential

# Drug_Target_1_GenAtlas_ID:
IL2RA

# Drug_Target_1_GenBank_ID_Gene:
X01057

# Drug_Target_1_GenBank_ID_Protein:
33813

# Drug_Target_1_GeneCard_ID:
IL2RA

# Drug_Target_1_Gene_Name:
IL2RA

# Drug_Target_1_Gene_Sequence:
>819 bp
ATGGATTCATACCTGCTGATGTGGGGACTGCTCACGTTCATCATGGTGCCTGGCTGCCAG
GCAGAGCTCTGTGACGATGACCCGCCAGAGATCCCACACGCCACATTCAAAGCCATGGCC
TACAAGGAAGGAACCATGTTGAACTGTGAATGCAAGAGAGGTTTCCGCAGAATAAAAAGC
GGGTCACTCTATATGCTCTGTACAGGAAACTCTAGCCACTCGTCCTGGGACAACCAATGT
CAATGCACAAGCTCTGCCACTCGGAACACAACGAAACAAGTGACACCTCAACCTGAAGAA
CAGAAAGAAAGGAAAACCACAGAAATGCAAAGTCCAATGCAGCCAGTGGACCAAGCGAGC
CTTCCAGGTCACTGCAGGGAACCTCCACCATGGGAAAATGAAGCCACAGAGAGAATTTAT
CATTTCGTGGTGGGGCAGATGGTTTATTATCAGTGCGTCCAGGGATACAGGGCTCTACAC
AGAGGTCCTGCTGAGAGCGTCTGCAAAATGACCCACGGGAAGACAAGGTGGACCCAGCCC
CAGCTCATATGCACAGGTGAAATGGAGACCAGTCAGTTTCCAGGTGAAGAGAAGCCTCAG
GCAAGCCCCGAAGGCCGTCCTGAGAGTGAGACTTCCTGCCTCGTCACAACAACAGATTTT
CAAATACAGACAGAAATGGCTGCAACCATGGAGACGTCCATATTTACAACAGAGTACCAG
GTAGCAGTGGCCGGCTGTGTTTTCCTGCTGATCAGCGTCCTCCTCCTGAGTGGGCTCACC
TGGCAGCGGAGACAGAGGAAGAGTAGAAGAACAATCTAG

# Drug_Target_1_General_Function:
Involved in interleukin-2 receptor activity

# Drug_Target_1_General_References:
2996141	Leonard WJ, Depper JM, Kanehisa M, Kronke M, Peffer NJ, Svetlik PB, Sullivan M, Greene WC: Structure of the human interleukin-2 receptor gene. Science. 1985 Nov 8;230(4726):633-9.
2999698	Ishida N, Kanamori H, Noma T, Nikaido T, Sabe H, Suzuki N, Shimizu A, Honjo T: Molecular cloning and structure of the human interleukin 2 receptor gene. Nucleic Acids Res. 1985 Nov 11;13(21):7579-89.
3030566	Cross SL, Feinberg MB, Wolf JB, Holbrook NJ, Wong-Staal F, Leonard WJ: Regulation of the human interleukin-2 receptor alpha chain promoter: activation of a nonfunctional promoter by the transactivator gene of HTLV-I. Cell. 1987 Apr 10;49(1):47-56.
3134887	Miedel MC, Hulmes JD, Weber DV, Bailon P, Pan YC: Structural analysis of recombinant soluble human interleukin-2 receptor. Primary structure, assignment of disulfide bonds and core IL-2 binding structure. Biochem Biophys Res Commun. 1988 Jul 15;154(1):372-9.
6090948	Leonard WJ, Depper JM, Crabtree GR, Rudikoff S, Pumphrey J, Robb RJ, Kronke M, Svetlik PB, Peffer NJ, Waldmann TA, et al.: Molecular cloning and expression of cDNAs for the human interleukin-2 receptor. Nature. 1984 Oct 18-24;311(5987):626-31.
6090949	Nikaido T, Shimizu A, Ishida N, Sabe H, Teshigawara K, Maeda M, Uchiyama T, Yodoi J, Honjo T: Molecular cloning of cDNA encoding human interleukin-2 receptor. Nature. 1984 Oct 18-24;311(5987):631-5.
7529123	Bamborough P, Hedgecock CJ, Richards WG: The interleukin-2 and interleukin-4 receptors studied by molecular modelling. Structure. 1994 Sep 15;2(9):839-51.

# Drug_Target_1_HGNC_ID:
HGNC:6008

# Drug_Target_1_HPRD_ID:
00986

# Drug_Target_1_ID:
724

# Drug_Target_1_Locus:
10p15-p14

# Drug_Target_1_Molecular_Weight:
30819

# Drug_Target_1_Name:
Interleukin-2 receptor alpha chain

# Drug_Target_1_Number_of_Residues:
276

# Drug_Target_1_PDB_ID:
Not Available

# Drug_Target_1_Pathway:
Not Available

# Drug_Target_1_Pfam_Domain_Function:
PF00084	Sushi

# Drug_Target_1_Protein_Sequence:
>Interleukin-2 receptor alpha chain precursor
MDSYLLMWGLLTFIMVPGCQAELCDDDPPEIPHATFKAMAYKEGTMLNCECKRGFRRIKS
GSLYMLCTGNSSHSSWDNQCQCTSSATRNTTKQVTPQPEEQKERKTTEMQSPMQPVDQAS
LPGHCREPPPWENEATERIYHFVVGQMVYYQCVQGYRALHRGPAESVCKMTHGKTRWTQP
QLICTGEMETSQFPGEEKPQASPEGRPESETSCLVTTTDFQIQTEMAATMETSIFTTEYQ
VAVAGCVFLLISVLLLSGLTWQRRQRKSRRTI

# Drug_Target_1_Reaction:
Not Available

# Drug_Target_1_Signals:
1-21

# Drug_Target_1_Specific_Function:
Receptor for interleukin-2

# Drug_Target_1_SwissProt_ID:
P01589

# Drug_Target_1_SwissProt_Name:
IL2RA_HUMAN

# Drug_Target_1_Synonyms:
CD25 antigen
IL-2 receptor alpha subunit
IL-2-RA
IL2-RA
Interleukin-2 receptor alpha chain precursor
TAC antigen
p55

# Drug_Target_1_Theoretical_pI:
6.49

# Drug_Target_1_Transmembrane_Regions:
241-259

# Drug_Target_2_Cellular_Location:
Membrane
single-pass type I membrane protein

# Drug_Target_2_Chromosome_Location:
Not Available

# Drug_Target_2_Drug_References:
11752352	Chen X, Ji ZL, Chen YZ: TTD: Therapeutic Target Database. Nucleic Acids Res. 2002 Jan 1;30(1):412-5.
15811959	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.
16516670	Foss F: Clinical experience with denileukin diftitox (ONTAK). Semin Oncol. 2006 Feb;33(1 Suppl 3):S11-6.
17187516	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.
18684057	Duvic M, Talpur R: Optimizing denileukin diftitox (Ontak) therapy. Future Oncol. 2008 Aug;4(4):457-69.

# Drug_Target_2_Essentiality:
Non-Essential

# Drug_Target_2_GenAtlas_ID:
IL2RB

# Drug_Target_2_GenBank_ID_Gene:
M26062

# Drug_Target_2_GenBank_ID_Protein:
307048

# Drug_Target_2_GeneCard_ID:
IL2RB

# Drug_Target_2_Gene_Name:
IL2RB

# Drug_Target_2_Gene_Sequence:
>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

# Drug_Target_2_General_Function:
Involved in hematopoietin/interferon-class (D200-domain) cytokine receptor activity

# Drug_Target_2_General_References:
10591208	Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95.
2785715	Hatakeyama M, Tsudo M, Minamoto S, Kono T, Doi T, Miyata T, Miyasaka M, Taniguchi T: Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA's. Science. 1989 May 5;244(4904):551-6.
7529123	Bamborough P, Hedgecock CJ, Richards WG: The interleukin-2 and interleukin-4 receptors studied by molecular modelling. Structure. 1994 Sep 15;2(9):839-51.

# Drug_Target_2_HGNC_ID:
HGNC:6009

# Drug_Target_2_HPRD_ID:
00896

# Drug_Target_2_ID:
717

# Drug_Target_2_Locus:
22q13|22q13.1

# Drug_Target_2_Molecular_Weight:
61118

# Drug_Target_2_Name:
Interleukin-2 receptor subunit beta

# Drug_Target_2_Number_of_Residues:
560

# Drug_Target_2_PDB_ID:
Not Available

# Drug_Target_2_Pathway:
Not Available

# Drug_Target_2_Pfam_Domain_Function:
Not Available

# Drug_Target_2_Protein_Sequence:
>Interleukin-2 receptor beta chain precursor
MAAPALSWRLPLLILLLPLATSWASAAVNGTSQFTCFYNSRANISCVWSQDGALQDTSCQ
VHAWPDRRRWNQTCELLPVSQASWACNLILGAPDSQKLTTVDIVTLRVLCREGVRWRVMA
IQDFKPFENLRLMAPISLQVVHVETHRCNISWEISQASHYFERHLEFEARTLSPGHTWEE
APLLTLKQKQEWICLETLTPDTQYEFQVRVKPLQGEFTTWSPWSQPLAFRTKPAALGKDT
IPWLGHLLVGLSGAFGFIILVYLLINCRNTGPWLKKVLKCNTPDPSKFFSQLSSEHGGDV
QKWLSSPFPSSSFSPGGLAPEISPLEVLERDKVTQLLLQQDKVPEPASLSSNHSLTSCFT
NQGYFFFHLPDALEIEACQVYFTYDPYSEEDPDEGVAGAPTGSSPQPLQPLSGEDDAYCT
FPSRDDLLLFSPSLLGGPSPPSTAPGGSGAGEERMPPSLQERVPRDWDPQPLGPPTPGVP
DLVDFQPPPELVLREAGEEVPDAGPREGVSFPWSRPPGQGEFRALNARLPLNTDAYLSLQ
ELQGQDPTHLV

# Drug_Target_2_Reaction:
Not Available

# Drug_Target_2_Signals:
1-26

# Drug_Target_2_Specific_Function:
Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2

# Drug_Target_2_SwissProt_ID:
P14784

# Drug_Target_2_SwissProt_Name:
IL2RB_HUMAN

# Drug_Target_2_Synonyms:
CD122 antigen
High affinity IL-2 receptor subunit beta
IL-2 receptor
Interleukin-2 receptor subunit beta precursor
P70-75
p75

# Drug_Target_2_Theoretical_pI:
4.68

# Drug_Target_2_Transmembrane_Regions:
241-265

# Drug_Target_3_Cellular_Location:
Membrane

# Drug_Target_3_Chromosome_Location:
Not Available

# Drug_Target_3_Drug_References:
11707860	Foss FM: DAB(389)IL-2 (denileukin diftitox, ONTAK): a new fusion protein technology. Clin Lymphoma. 2000 Nov;1 Suppl 1:S27-31.
15811959	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.
16516670	Foss F: Clinical experience with denileukin diftitox (ONTAK). Semin Oncol. 2006 Feb;33(1 Suppl 3):S11-6.

# Drug_Target_3_Essentiality:
Non-Essential

# Drug_Target_3_GenAtlas_ID:
IL2RG

# Drug_Target_3_GenBank_ID_Gene:
D11086

# Drug_Target_3_GenBank_ID_Protein:
219890

# Drug_Target_3_GeneCard_ID:
IL2RG

# Drug_Target_3_Gene_Name:
IL2RG

# Drug_Target_3_Gene_Sequence:
>1110 bp
ATGTTGAAGCCATCATTACCATTCACATCCCTCTTATTCCTGCAGCTGCCCCTGCTGGGA
GTGGGGCTGAACACGACAATTCTGACGCCCAATGGGAATGAAGACACCACAGCTGATTTC
TTCCTGACCACTATGCCCACTGACTCCCTCAGTGTTTCCACTCTGCCCCTCCCAGAGGTT
CAGTGTTTTGTGTTCAATGTCGAGTACATGAATTGCACTTGGAACAGCAGCTCTGAGCCC
CAGCCTACCAACCTCACTCTGCATTATTGGTACAAGAACTCGGATAATGATAAAGTCCAG
AAGTGCAGCCACTATCTATTCTCTGAAGAAATCACTTCTGGCTGTCAGTTGCAAAAAAAG
GAGATCCACCTCTACCAAACATTTGTTGTTCAGCTCCAGGACCCACGGGAACCCAGGAGA
CAGGCCACACAGATGCTAAAACTGCAGAATCTGGTGATCCCCTGGGCTCCAGAGAACCTA
ACACTTCACAAACTGAGTGAATCCCAGCTAGAACTGAACTGGAACAACAGATTCTTGAAC
CACTGTTTGGAGCACTTGGTGCAGTACCGGACTGACTGGGACCACAGCTGGACTGAACAA
TCAGTGGATTATAGACATAAGTTCTCCTTGCCTAGTGTGGATGGGCAGAAACGCTACACG
TTTCGTGTTCGGAGCCGCTTTAACCCACTCTGTGGAAGTGCTCAGCATTGGAGTGAATGG
AGCCACCCAATCCACTGGGGGAGCAATACTTCAAAAGAGAATCCTTTCCTGTTTGCATTG
GAAGCCGTGGTTATCTCTGTTGGCTCCATGGGATTGATTATCAGCCTTCTCTGTGTGTAT
TTCTGGCTGGAACGGACGATGCCCCGAATTCCCACCCTGAAGAACCTAGAGGATCTTGTT
ACTGAATACCACGGGAACTTTTCGGCCTGGAGTGGTGTGTCTAAGGGACTGGCTGAGAGT
CTGCAGCCAGACTACAGTGAACGACTCTGCCTCGTCAGTGAGATTCCCCCAAAAGGAGGG
GCCCTTGGGGAGGGGCCTGGGGCCTCCCCATGCAACCAGCATAGCCCCTACTGGGCCCCC
CCATGTTACACCCTAAAGCCTGAAACCTGA

# Drug_Target_3_General_Function:
Not Available

# Drug_Target_3_General_References:
1631559	Takeshita T, Asao H, Ohtani K, Ishii N, Kumaki S, Tanaka N, Munakata H, Nakamura M, Sugamura K: Cloning of the gamma chain of the human IL-2 receptor. Science. 1992 Jul 17;257(5068):379-82.
8266076	Kondo M, Takeshita T, Ishii N, Nakamura M, Watanabe S, Arai K, Sugamura K: Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4. Science. 1993 Dec 17;262(5141):1874-7.
8266077	Noguchi M, Nakamura Y, Russell SM, Ziegler SF, Tsang M, Cao X, Leonard WJ: Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor. Science. 1993 Dec 17;262(5141):1877-80.
8266078	Russell SM, Keegan AD, Harada N, Nakamura Y, Noguchi M, Leland P, Friedmann MC, Miyajima A, Puri RK, Paul WE, et al.: Interleukin-2 receptor gamma chain: a functional component of the interleukin-4 receptor. Science. 1993 Dec 17;262(5141):1880-3.
8401490	Puck JM, Deschenes SM, Porter JC, Dutra AS, Brown CJ, Willard HF, Henthorn PS: The interleukin-2 receptor gamma chain maps to Xq13.1 and is mutated in X-linked severe combined immunodeficiency, SCIDX1. Hum Mol Genet. 1993 Aug;2(8):1099-104.
8514792	Noguchi M, Adelstein S, Cao X, Leonard WJ: Characterization of the human interleukin-2 receptor gamma chain gene. J Biol Chem. 1993 Jun 25;268(18):13601-8.

# Drug_Target_3_HGNC_ID:
HGNC:6010

# Drug_Target_3_HPRD_ID:
Not Available

# Drug_Target_3_ID:
3823

# Drug_Target_3_Locus:
Xq13.1

# Drug_Target_3_Molecular_Weight:
42287

# Drug_Target_3_Name:
Cytokine receptor common gamma chain

# Drug_Target_3_Number_of_Residues:
375

# Drug_Target_3_PDB_ID:
Not Available

# Drug_Target_3_Pathway:
Not Available

# Drug_Target_3_Pfam_Domain_Function:
Not Available

# Drug_Target_3_Protein_Sequence:
>Cytokine receptor common gamma chain
MLKPSLPFTSLLFLQLPLLGVGLNTTILTPNGNEDTTADFFLTTMPTDSLSVSTLPLPEV
QCFVFNVEYMNCTWNSSSEPQPTNLTLHYWYKNSDNDKVQKCSHYLFSEEITSGCQLQKK
EIHLYQTFVVQLQDPREPRRQATQMLKLQNLVIPWAPENLTLHKLSESQLELNWNNRFLN
HCLEHLVQYRTDWDHSWTEQSVDYRHKFSLPSVDGQKRYTFRVRSRFNPLCGSAQHWSEW
SHPIHWGSNTSKENPFLFALEAVVISVGSMGLIISLLCVYFWLERTMPRIPTLKNLEDLV
TEYHGNFSAWSGVSKGLAESLQPDYSERLCLVSEIPPKGGALGEGPGASPCNQHSPYWAP
PCYTLKPET

# Drug_Target_3_Reaction:
Not Available

# Drug_Target_3_Signals:
1-22

# Drug_Target_3_Specific_Function:
Common subunit for the receptors for a variety of interleukins

# Drug_Target_3_SwissProt_ID:
P31785

# Drug_Target_3_SwissProt_Name:
IL2RG_HUMAN

# Drug_Target_3_Synonyms:
CD132 antigen
Cytokine receptor common gamma chain precursor
Gamma-C
IL-2R gamma chai