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Showing drug card for Palivizumab (DB00110)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-05-26 16:10:00
Primary Accession Number DB00110
Secondary Accession Number
  • BIOD00097
  • BTD00097
Name Palivizumab
Drug Type
  • Approved
  • Biotech
  • Investigational
Description Humanized monoclonal antibody (IgG1k) produced by recombinant DNA technology, directed to an epitope in the A antigenic site of the F protein of respiratory syncytial virus (RSV). Synagis is a composite of human (95%) and murine (5%) antibody sequences. The human heavy chain sequence was derived from the constant domains of human IgG1 and the variable framework regions of the VH genes Cor (1) and Cess (2). The human lightchain sequence was derived from the constant domain of Ck and the variable framework regions of the VL gene K104 withJk-4. Palivizumab is expressed from a stable murine (mouse) myeloma cell line (NS0). Palivizumab is composed of to heavy chains (50.6 kDa each) and two light chains (27.6 kDa each), contains 1-2% carbohydrate by weight and has a molecular weight of 147.7 kDa +/- 1 kDa (MALDI-TOF)
Synonyms
  1. Synagis
  2. anti-RSV
  3. palivizumab
Brand Names
  1. Synagis
Brand Mixtures Not Available
Chemical IUPAC Name Humanized anti-RSV antibody
Chemical Formula Not Available
Chemical Structure Structure
Protein Sequence(s) >VH Region 
QVTLRESGPALVKPTQTLTLTCTFSGFSLSTSGMSVGWIRQPPGKALEWLADIWWDDKKD
YNPSLKSRLTISKDTSKNQVVLKVTNMDPADTATYYCARSMITNWYFDVWGAGTTVTVSS

>VH region MEDI-493 
QVTLRESGPALVKPTQTLTLTCTFSGFSLSTSGMSVGWIRQPPGKALEWLADIWWDDKKD
YNPSLKSRLTISKDTSKNQVVLKVTNMDPADTATYYCARSMITNWYFDVWGAGTTVTVSS
CAS Registry Number 188039-54-5
InChI Identifier Not Available
InChI Key Not Available
KEGG Drug Not Available
KEGG Compound Not Available
PubChem Compound Not Available
PubChem Substance Not Available
ChEBI ID Not Available
PharmGKB ID PA450764 Link Image
HET ID Not Available
GenBank ID Not Available
Drug ID Number [DIN] 02245889 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/palivizumab.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Palivizumab Link Image
FDA Label
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Sequence listed in Johnson S, Oliver C, Prince GA, Hemming VG, Pfarr DS, Wang SC, Dormitzer M, O'Grady J, Koenig S, Tamura JK, Woods R, Bansal G, Couchenour D, Tsao E, Hall WC, Young JF. Development of a humanized monoclonal antibody (MEDI-493) with potent in vitro and in vivo activity against respiratory syncytial virus. J Infect Dis. 1997 Nov;176(5):1215-24.
Average Molecular Weight Not Available
Monoisotopic Molecular Weight Not Available
State Liquid
Melting Point 61 oC (FAB fragment), 71 oC (whole mAb) - Vermeer, A.W.P. & Norde, W., Biophys. J. 78:394-404 (2000).
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP Not Available Calculated using ALOGPS
Experimental LogS Not Available
Predicted LogS Not Available Calculated using ALOGPS
Experimental Caco2 Permeability Not Available
pKa/Isoelectric Point Not Available
Mass Spectrum Not Available
MOL File Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID 1IGT Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category
  • Antiviral Agents
ATC Codes
AHFS Codes
  • 08:18.24
Indication For treatment of respiratory diseases casued by respiratory syncytial virus
Pharmacology Synagis exhibits neutralizing and fusion-inhibitory activity against Respiratory syncytial virus (RSV). These activities inhibit RSV replication or spread. Synagis is given to prevent the development of lower respiratory tract disease in pediatric patients.
Mechanism of Action Binds to the outer coat or Fusion glycoprotein of RSV. This prevents its binding and uptake by host cellular receptors.
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Most likely removed by opsonization via the reticuloendothelial system.
Half Life 18-20 days (in adults)
Dosage Forms
Form Route
Powder, for solution Intramuscular
Patient Information Not Available
Contraindications Show Link Image
Interactions Show Link Image
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Drugs.com Link Image
  2. Wikipedia Link Image
  3. RxList Link Image
Organisms Affected Not Available
Targets
  1. Fusion glycoprotein F0
  2. High affinity immunoglobulin gamma Fc receptor I
  3. Low affinity immunoglobulin gamma Fc region receptor III-B
  4. Complement C1r subcomponent
  5. Complement C1q subcomponent subunit A
  6. Complement C1q subcomponent subunit B
  7. Complement C1q subcomponent subunit C
  8. Low affinity immunoglobulin gamma Fc region receptor III-A
  9. Low affinity immunoglobulin gamma Fc region receptor II-a
  10. Low affinity immunoglobulin gamma Fc region receptor II-b
  11. Low affinity immunoglobulin gamma Fc region receptor II-c
Drug Target 1 [top]
Target 1 ID 757
Target 1 Name Fusion glycoprotein F0
Target 1 Synonyms
  1. Fusion glycoprotein F0 precursor
Target 1 Gene Name F
Target 1 Protein Sequence >Fusion glycoprotein F0 precursor [Contains: Fusion glycoprotein F2; Fusion glycoprotein F1] 
MELLIHRSSAIFLTLAVNALYLTSSQNITEEFYQSTCSAVSRGYFSALRTGWYTSVITIE
LSNIKETKCNGTDTKVKLIKQELDKYKNAVTELQLLMQNTPAANNRARREAPQYMNYTIN
TTKNLNVSISKKRKRRFLGFLLGVGSAIASGIAVSKVLHLEGEVNKIKNALLSTNKAVVS
LSNGVSVLTSKVLDLKNYINNRLLPIVNQQSCRISNIETVIEFQQMNSRLLEITREFSVN
AGVTTPLSTYMLTNSELLSLINDMPITNDQKKLMSSNVQIVRQQSYSIMSIIKEEVLAYV
VQLPIYGVIDTPCWKLHTSPLCTTNIKEGSNICLTRTDRGWYCDNAGSVSFFPQADTCKV
QSNRVFCDTMNSLTLPSEVSLCNTDIFNSKYDCKIMTSKTDISSSVITSLGAIVSCYGKT
KCTASNKNRGIIKTFSNGCDYVSNKGVDTVSVGNTLYYVNKLEGKNLYVKGEPIINYYDP
LVFPSDEFDASISQVNEKINQSLAFIRRSDELLHNVNTGKSTTNIMITTIIIVIIVVLLS
LIAIGLLLYCKAKNTPVTLSKDQLSGINNIAFSK
Target 1 Number of Residues 583
Target 1 Molecular Weight 63689
Target 1 Theoretical pI 9.14
Target 1 GO Classification
Function
Not Available
Process
physiological process
cellular physiological process
syncytium formation
syncytium formation by plasma membrane fusion
induction by virus of cell-cell fusion in host
Component
Not Available
Target 1 General Function Not Available
Target 1 Specific Function Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states:pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C- terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with HN at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis
Target 1 Pathways Not Available
Target 1 Reactions Not Available
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-22
Target 1 Transmembrane Regions
  • 530-550
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 222565 Link Image
Target 1 UniProtKB/Swiss-Prot ID P13843 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name FUS_HRSV1 Link Image
Target 1 PDB ID 1G2C Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Membrane
  • single-pass type I membrane protein
Target 1 Gene Sequence >1725 bp 
ATGGAGTTGCTGATCCACAGGTCAAGTGCAATCTTCCTAACTCTTGCTGTTAATGCATTG
TACCTCACCTCAAGTCAGAACATAACTGAGGAGTTTTACCAATCGACATGTAGTGCAGTT
AGCAGAGGTTATTTTAGTGCTTTAAGAACAGGTTGGTATACCAGTGTCATAACAATAGAA
TTAAGTAATATAAAAGAAACCAAATGCAATGGAACTGACACTAAAGTAAAACTTATAAAA
CAAGAATTAGATAAGTATAAGAATGCAGTAACAGAATTACAGCTACTTATGCAAAACACG
CCAGCTGCCAACAACCGGGCCAGAAGAGAAGCACCACAGTACATGAACTACACAATCAAT
ACCACAAAAAACCTAAATGTATCAATAAGCAAGAAAAGGAAACGAAGATTTCTGGGCTTC
TTGTTAGGTGTAGGATCTGCAATAGCAAGTGGTATAGCTGTATCCAAAGTTTTACACCTT
GAAGGAGAAGTGAACAAAATCAAAAATGCTTTGTTGTCTACAAACAAAGCTGTAGTCAGT
CTATCAAATGGGGTCAGTGTTTTAACCAGCAAAGTGTTAGATCTCAAGAATTACATAAAT
AACCGATTATTACCCATAGTAAATCAACAGAGCTGTCGCATCTCCAACATTGAAACAGTT
ATAGAATTCCAGCAGATGAATAGCAGATTGTTGGAAATCACCAGAGAATTTAGTGTTAAT
GCAGGTGTAACAACACCTTTAAGCACTTACATGTTAACAAACAGTGAGTTACTATCATTG
ATCAATGATATGCCTATAACAAATGACCAGAAAAAATTAATGTCAAGCAATGTTCAGATA
GTAAGGCAACAAAGTTATTCTATCATGTCTATAATAAAGGAAGAAGTCCTTGCATATGTT
GTACAGCTACCTATCTATGGTGTAATAGATACACCTTGCTGGAAATTACACACATCACCT
CTATGCACCACCAACATCAAAGAAGGATCAAATATTTGTTTAACAAGGACTGATAGAGGA
TGGTATTGTGATAATGCAGGATCAGTATCCTTCTTCCCACAGGCTGATACTTGCAAAGTA
CAGTCCAATCGAGTATTTTGTGACACTATGAACAGTTTAACATTACCAAGTGAAGTCAGC
CTTTGTAACACTGACATATTCAATTCCAAGTATGACTGCAAAATTATGACATCAAAAACA
GACATAAGCAGCTCAGTAATTACTTCTCTTGGAGCTATAGTGTCATGCTATGGAAAAACT
AAATGCACTGCATCCAATAAAAATCGTGGGATTATAAAGACATTTTCTAATGGTTGTGAC
TATGTGTCAAACAAAGGAGTAGATACTGTGTCAGTGGGCAACACTTTATACTATGTAAAC
AAGCTGGAAGGCAAAAACCTTTATGTAAAAGGGGAACCTATAATAAATTACTATGATCCT
CTAGTGTTTCCTTCTGATGAGTTTGATGCATCAATATCTCAAGTCAATGAAAAAATCAAT
CAAAGTTTAGCTTTTATTCGTAGATCTGATGAATTACTACATAATGTAAATACTGGCAAA
TCTACTACAAATATTATGATAACTACAATTATTATAGTAATCATTGTAGTATTGTTATCA
TTAATAGCTATTGGTTTACTGTTGTATTGCAAAGCCAAAAACACACCAGTTACACTAAGC
AAAGACCAACTAAGTGGAATCAATAATATTGCATTCAGCAAATAG
Target 1 GenBank Gene ID
Target 1 GeneCard ID Not Available
Target 1 GenAtlas ID Not Available
Target 1 HGNC ID Not Available
Target 1 Chromosome Location Not Available
Target 1 Locus Not Available
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. Johnson PR, Collins PL: The fusion glycoproteins of human respiratory syncytial virus of subgroups A and B: sequence conservation provides a structural basis for antigenic relatedness. J Gen Virol. 1988 Oct;69 ( Pt 10):2623-8. [PubMed Link Image]
Target 1 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 784
Target 2 Name High affinity immunoglobulin gamma Fc receptor I
Target 2 Synonyms
  1. CD64 antigen
  2. Fc-gamma RI
  3. FcRI
  4. High affinity immunoglobulin gamma Fc receptor I precursor
  5. IgG Fc receptor I
Target 2 Gene Name FCGR1A
Target 2 Protein Sequence >High affinity immunoglobulin gamma Fc receptor I precursor 
MWFLTTLLLWVPVDGQVDTTKAVITLQPPWVSVFQEETVTLHCEVLHLPGSSSTQWFLNG
TATQTSTPSYRITSASVNDSGEYRCQRGLSGRSDPIQLEIHRGWLLLQVSSRVFTEGEPL
ALRCHAWKDKLVYNVLYYRNGKAFKFFHWNSNLTILKTNISHNGTYHCSGMGKHRYTSAG
ISVTVKELFPAPVLNASVTSPLLEGNLVTLSCETKLLLQRPGLQLYFSFYMGSKTLRGRN
TSSEYQILTARREDSGLYWCEAATEDGNVLKRSPELELQVLGLQLPTPVWFHVLFYLAVG
IMFLVNTVLWVTIRKELKRKKKWDLEISLDSGHEKKVISSLQEDRHLEEELKCQEQKEEQ
LQEGVHRKEPQGAT
Target 2 Number of Residues 380
Target 2 Molecular Weight 42632
Target 2 Theoretical pI 8.08
Target 2 GO Classification Not Available
Target 2 General Function Involved in receptor signaling protein activity
Target 2 Specific Function Binds to the Fc region of immunoglobulins gamma. High affinity receptor
Target 2 Pathways Not Available
Target 2 Reactions Not Available
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-15
Target 2 Transmembrane Regions
  • 293-313
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 31332 Link Image
Target 2 UniProtKB/Swiss-Prot ID P12314 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name FCGR1_HUMAN Link Image
Target 2 PDB ID Not Available
Target 2 Cellular Location
  • Membrane
  • single-pass type I membrane protein
Target 2 Gene Sequence >1125 bp 
ATGTGGTTCTTGACAACTCTGCTCCTTTGGGTTCCAGTTGATGGGCAAGTGGACACCACA
AAGGCAGTGATCTCTTTGCAGCCTCCATGGGTCAGCGTGTTCCAAGAGGAAACCGTAACC
TTGCACTGTGAGGTGCTCCATCTGCCTGGGAGCAGCTCTACACAGTGGTTTCTCAATGGC
ACAGCCACTCAGACCTCGACCCCCAGCTACAGAATCACCTCTGCCAGTGTCAATGACAGT
GGTGAATACAGGTGCCAGAGAGGTCTCTCAGGGCGAAGTGACCCCATACAGCTGGAAATC
CACAGAGGCTGGCTACTACTGCAGGTCTCCAGCAGAGTCTTCACGGAAGGAGAACCTCTG
GCCTTGAGGTGTCATGCGTGGAAGGATAAGCTGGTGTACAATGTGCTTTACTATCGAAAT
GGCAAAGCCTTTAAGTTTTTCCACTGGAATTCTAACCTCACCATTCTGAAAACCAACATA
AGTCACAATGGCACCTACCATTGCTCAGGCATGGGAAAGCATCGCTACACATCAGCAGGA
ATATCTGTCACTGTGAAAGAGCTATTTCCAGCTCCAGTGCTGAATGCATCTGTGACATCC
CCACTCCTGGAGGGGAATCTGGTCACCCTGAGCTGTGAAACAAAGTTGCTCTTGCAGAGG
CCTGGTTTGCAGCTTTACTTCTCCTTCTACATGGGCAGCAAGACCCTGCGAGGCAGGAAC
ACATCCTCTGAATACCAAATACTAACTGCTAGAAGAGAAGACTCTGGGTTATACTGGTGC
GAGGCTGCCACAGAGGATGGAAATGTCCTTAAGCGCAGCCCTGAGTTGGAGCTTCAAGTG
CTTGGCCTCCAGTTACCAACTCCTGTCTGGTTTCATGTCCTTTTCTATCTGGCAGTGGGA
ATAATGTTTTTAGTGAACACTGTTCTCTGGGTGACAATACGTAAAGAACTGAAAAGAAAG
AAAAAGTGGGATTTAGAAATCTCTTTGGATTCTGGTCATGAGAAGAAGGTAACTTCCAGC
CTTCAAGAAGACAGACATTTAGAAGAAGAGCTGAAATGTCAGGAACAAAAAGAAGAACAG
CTGCAGGAAGGGGTGCACCGGAAGGAGCCCCAGGGGGCCACGTAG
Target 2 GenBank Gene ID
Target 2 GeneCard ID FCGR1A Link Image
Target 2 GenAtlas ID FCGR1A Link Image
Target 2 HGNC ID HGNC:3613 Link Image
Target 2 Chromosome Location 1
Target 2 Locus 1q21.2-q21.3
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. Allen JM, Seed B: Isolation and expression of functional high-affinity Fc receptor complementary DNAs. Science. 1989 Jan 20;243(4889):378-81. [PubMed Link Image]
  5. 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. [PubMed Link Image]
Target 2 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 1102
Target 3 Name Low affinity immunoglobulin gamma Fc region receptor III-B
Target 3 Synonyms
  1. CD16b antigen
  2. Fc-gamma RIII
  3. Fc-gamma RIII-beta
  4. Fc-gamma RIIIb
  5. FcR-10
  6. FcRIII
  7. FcRIIIb
  8. IgG Fc receptor III-1
  9. Low affinity immunoglobulin gamma Fc region receptor III-B precursor
Target 3 Gene Name FCGR3B
Target 3 Protein Sequence >Low affinity immunoglobulin gamma Fc region receptor III-B precursor 
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYSVLEKDSVTLKCQGAYSPEDNSTQW
FHNESLISSQASSYFIDAATVNDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE
EDPIHLRCHSWKNTALHKVTYLQNGKDRKYFHHNSDFHIPKATLKDSGSYFCRGLVGSKN
VSSETVNITITQGLAVSTISSFSPPGYQVSFCLVMVLLFAVDTGLYFSVKTNI
Target 3 Number of Residues 236
Target 3 Molecular Weight 26216
Target 3 Theoretical pI 6.71
Target 3 GO Classification Not Available
Target 3 General Function Not Available
Target 3 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
Target 3 Pathways Not Available
Target 3 Reactions Not Available
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-16
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 31322 Link Image
Target 3 UniProtKB/Swiss-Prot ID O75015 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name FCG3B_HUMAN Link Image
Target 3 PDB ID 1E4K Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Cell membrane
  • GPI-anchor. Secreted protein. Note=Secreted after cleavage
  • lipid-anchor
Target 3 Gene Sequence >702 bp 
ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT
GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGCGTGCTTGAGAAG
GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG
TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA
GTCAACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG
CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG
GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA
TATTTACAGAATGGCAAAGACAGGAAGTATTTTCATCATAATTCTGACTTCCACATTCCA
AAAGCCACACTCAAAGATAGCGGCTCCTACTTCTGCAGGGGGCTTGTTGGGAGTAAAAAT
GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA
TCATTCTCTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA
GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTTGA
Target 3 GenBank Gene ID
Target 3 GeneCard ID FCGR3B Link Image
Target 3 GenAtlas ID FCGR3B Link Image
Target 3 HGNC ID HGNC:3620 Link Image
Target 3 Chromosome Location 1
Target 3 Locus 1q23
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
  6. 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. [PubMed Link Image]
  7. 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. [PubMed Link Image]
  8. 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. [PubMed Link Image]
Target 3 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 3814
Target 4 Name Complement C1r subcomponent
Target 4 Synonyms
  1. Complement C1r subcomponent precursor
  2. Complement component 1, r subcomponent
  3. EC 3.4.21.41
Target 4 Gene Name C1R
Target 4 Protein Sequence >Complement C1r subcomponent 
MWLLYLLVPALFCRAGGSIPIPQKLFGEVTSPLFPKPYPNNFETTTVITVPTGYRVKLVF
QQFDLEPSEGCFYDYVKISADKKSLGRFCGQLGSPLGNPPGKKEFMSQGNKMLLTFHTDF
SNEENGTIMFYKGFLAYYQAVDLDECASRSKSGEEDPQPQCQHLCHNYVGGYFCSCRPGY
ELQEDRHSCQAECSSELYTEASGYISSLEYPRSYPPDLRCNYSIRVERGLTLHLKFLEPF
DIDDHQQVHCPYDQLQIYANGKNIGEFCGKQRPPDLDTSSNAVDLLFFTDESGDSRGWKL
RYTTEIIKCPQPKTLDEFTIIQNLQPQYQFRDYFIATCKQGYQLIEGNQVLHSFTAVCQD
DGTWHRAMPRCKIKDCGQPRNLPNGDFRYTTTMGVNTYKARIQYYCHEPYYKMQTRAGSR
ESEQGVYTCTAQGIWKNEQKGEKIPRCLPVCGKPVNPVEQRQRIIGGQKAKMGNFPWQVF
TNIHGRGGGALLGDRWILTAAHTLYPKEHEAQSNASLDVFLGHTNVEELMKLGNHPIRRV
SVHPDYRQDESYNFEGDIALLELENSVTLGPNLLPICLPDNDTFYDLGLMGYVSGFGVME
EKIAHDLRFVRLPVANPQACENWLRGKNRMDVFSQNMFCAGHPSLKQDACQGDSGGVFAV
RDPNTDRWVATGIVSWGIGCSRGYGFYTKVLNYVDWIKKEMEEED
Target 4 Number of Residues 716
Target 4 Molecular Weight 80174
Target 4 Theoretical pI 6.24
Target 4 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
binding
ion binding
cation binding
calcium ion binding
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
response to stimulus
response to biotic stimulus
defense response
immune response
humoral immune response
complement activation
Component
extracellular region
Target 4 General Function Not Available
Target 4 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
Target 4 Pathways
Name SMPDB Link KEGG Link
Complement and coagulation cascades map04610 Link Image
Target 4 Reactions
  • 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)))
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-17
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 29539 Link Image
Target 4 UniProtKB/Swiss-Prot ID P00736 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name C1R_HUMAN Link Image
Target 4 PDB ID 1GPZ Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cytoplasmic
Target 4 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
Target 4 GenBank Gene ID
Target 4 GeneCard ID C1R Link Image
Target 4 GenAtlas ID C1R Link Image
Target 4 HGNC ID HGNC:1246 Link Image
Target 4 Chromosome Location 12
Target 4 Locus 12p13
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
  6. 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. [PubMed Link Image]
  7. 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. [PubMed Link Image]
Target 4 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 5 [top]
Target 5 ID 3815
Target 5 Name Complement C1q subcomponent subunit A
Target 5 Synonyms
  1. Complement C1q subcomponent subunit A precursor
Target 5 Gene Name C1QA
Target 5 Protein Sequence >Complement C1q subcomponent subunit A 
MEGPRGWLVLCVLAISLASMVTEDLCRAPDGKKGEAGRPGRRGRPGLKGEQGEPGAPGIR
TGIQGLKGDQGEPGPSGNPGKVGYPGPSGPLGARGIPGIKGTKGSPGNIKDQPRPAFSAI
RRNPPMGGNVVIFDTVITNQEEPYQNHSGRFVCTVPGYYYFTFQVLSQWEICLSIVSSSR
GQVRRSLGFCDTTNKGLFQVVSGGMVLQLQQGDQVWVEKDPKKGHIYQGSEADSVFSGFL
IFPSA
Target 5 Number of Residues 249
Target 5 Molecular Weight 26017
Target 5 Theoretical pI 9.45
Target 5 GO Classification
Function
Not Available
Process
physiological process
cellular physiological process
transport
ion transport
anion transport
inorganic anion transport
phosphate transport
Component
cell
intracellular
cytoplasm
Target 5 General Function Not Available
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
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • 1-22
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 4894854 Link Image
Target 5 UniProtKB/Swiss-Prot ID P02745 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name C1QA_HUMAN Link Image
Target 5 PDB ID 1PK6 Link Image
Target 5 PDB File Show
Target 5 3D Structure
Target 5 Cellular Location
  • Secreted protein
Target 5 Gene Sequence >738 bp 
ATGGAGGGTCCCCGGGGATGGCTGGTGCTCTGTGTGCTGGCCATATCGCTGGCCTCTATG
GTGACCGAGGACTTGTGCCGAGCACCAGACGGGAAGAAAGGGGAGGCAGGAAGACCTGGC
AGACGGGGGCGGCCAGGCCTCAAGGGGGAGCAAGGGGAGCCGGGGGCCCCTGGCATCCGG
ACAGGCATCCAAGGCCTTAAAGGAGACCAGGGGGAACCTGGGCCCTCTGGAAACCCCGGC
AAGGTGGGCTACCCAGGGCCCAGCGGCCCCCTCGGGGCCCGTGGCATCCCGGGAATTAAA
GGCACCAAGGGCAGCCCAGGAAACATCAAGGACCAGCCGAGGCCAGCCTTCTCCGCCATT
CGGCGGAACCCCCCAATGGGGGGCAACGTGGTCATCTTCGACACGGTCATCACCAACCAG
GAAGAACCGTACCAGAACCACTCCGGCCGATTCGTCTGCACTGTACCCGGCTACTACTAC
TTCACCTTCCAGGTGCTGTCCCAGTGGGAAATCTGCCTGTCCATCGTCTCCTCCTCAAGG
GGCCAGGTCCGACGCTCCCTGGGCTTCTGTGACACCACCAACAAGGGGCTCTTCCAGGTG
GTGTCAGGGGGCATGGTGCTTCAGCTGCAGCAGGGTGACCAGGTCTGGGTTGAAAAAGAC
CCCAAAAAGGGTCACATTTACCAGGGCTCTGAGGCCGACAGCGTCTTCAGCGGCTTCCTC
ATCTTCCCATCTGCCTGA
Target 5 GenBank Gene ID
Target 5 GeneCard ID C1QA Link Image
Target 5 GenAtlas ID C1QA Link Image
Target 5 HGNC ID HGNC:1241 Link Image
Target 5 Chromosome Location 1
Target 5 Locus 1p36.12
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94. [PubMed Link Image]
Target 5 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 3816
Target 6 Name Complement C1q subcomponent subunit B
Target 6 Synonyms
  1. Complement C1q subcomponent subunit B precursor
Target 6 Gene Name C1QB
Target 6 Protein Sequence >Complement C1q subcomponent subunit B 
MKIPWGSIPVLMLLLLLGLIDISQAQLSCTGPPAIPGIPGIPGTPGPDGQPGTPGIKGEK
GLPGLAGDHGEFGEKGDPGIPGNPGKVGPKGPMGPKGGPGAPGAPGPKGESGDYKATQKI
AFSATRTINVPLRRDQTIRFDHVITNMNNNYEPRSGKFTCKVPGLYYFTYHASSRGNLCV
NLMRGRERAQKVVTFCDYAYNTFQVTTGGMVLKLEQGENVFLQATDKNSLLGMEGANSIF
SGFLLFPDMEA
Target 6 Number of Residues 255
Target 6 Molecular Weight 26460
Target 6 Theoretical pI 8.87
Target 6 GO Classification
Function
Not Available
Process
physiological process
cellular physiological process
transport
ion transport
anion transport
inorganic anion transport
phosphate transport
Component
cell
intracellular
cytoplasm
Target 6 General Function Not Available
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
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • 1-25
Target 6 Transmembrane Regions
  • None
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 573114 Link Image
Target 6 UniProtKB/Swiss-Prot ID P02746 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name C1QB_HUMAN Link Image
Target 6 PDB ID 1PK6 Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Secreted protein
Target 6 Gene Sequence >688 bp 
CCAGGCCCAGCTCAGCTGCACCGGGCCCCCAGCCATCCCTGGCATCCCGGGTATCCCTGG
GACACCTGGCCCCGATGGCCAACCTGGGACCCCAGGGATAAAAGGAGAGAAAGGGCTTCC
AGGGCTGGCTGGAGACCATGGTGAGTTCGGAGAGAAGGGAGACCCAGGGATTCCTGGGAA
TCCAGGAAAAGTCGGCCCCAAGGGCCCCATGGGCCCTAAAGGTGGCCCAGGGGCCCCTGG
AGCCCCAGGCCCCAAAGGTGAATCGGGAGACTACAAGGCCACCCAGAAAATCGCCTTCTC
TGCCACAAGAACCATCAACGTCCCCCTGCGCCGGGACCAGACCATCCGCTTCGACCACGT
GATCACCAACATGAACAACAATTATGAGCCCCGCAGTGGCAAGTTCACCTGCAAGGTGCC
CGGTCTCTACTACTTCACCTACCACGCCAGCTCTCGAGGGAACCTGTGCGTGAACCTCAT
GCGTGGCCGGGAGCGTGCACAGAAGGTGGTCACCTTCTGTGACTATGCCTACAACACCTT
CCAGGTCACCACCGGTGGCATGGTCCTCAAGCTGGAGCAGGGGGAGAACGTCTTCCTGCA
GGCCACCGACAAGAACTCACTACTGGGCATGGAGGGTGCCAACAGCATCTTTTCCGGGTT
CCTGCTCTTTCCAGATATGGAGGCCTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID C1QB Link Image
Target 6 GenAtlas ID C1QB Link Image
Target 6 HGNC ID HGNC:1242 Link Image
Target 6 Chromosome Location 1
Target 6 Locus 1p36.12
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
  6. 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. [PubMed Link Image]
  7. Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94. [PubMed Link Image]
Target 6 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 3817
Target 7 Name Complement C1q subcomponent subunit C
Target 7 Synonyms
  1. Complement C1q subcomponent subunit C precursor
Target 7 Gene Name C1QC
Target 7 Protein Sequence >Complement C1q subcomponent subunit C 
MDVGPSSLPHLGLKLLLLLLLLPLRGQANTGCYGIPGMPGLPGAPGKDGYDGLPGPKGEP
GIPAIPGIRGPKGQKGEPGLPGHPGKNGPMGPPGMPGVPGPMGIPGEPGEEGRYKQKFQS
VFTVTRQTHQPPAPNSLIRFNAVLTNPQGDYDTSTGKFTCKVPGLYYFVYHASHTANLCV
LLYRSGVKVVTFCGHTSKTNQVNSGGVLLRLQVGEEVWLAVNDYYDMVGIQGSDSVFSGF
LLFPD
Target 7 Number of Residues 249
Target 7 Molecular Weight 25774
Target 7 Theoretical pI 8.58
Target 7 GO Classification
Function
Not Available
Process
physiological process
cellular physiological process
transport
ion transport
anion transport
inorganic anion transport
phosphate transport
Component
cell
intracellular
cytoplasm
Target 7 General Function Not Available
Target 7 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
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • 1-28
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 33150626 Link Image
Target 7 UniProtKB/Swiss-Prot ID P02747 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name C1QC_HUMAN Link Image
Target 7 PDB ID 1PK6 Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location
  • Secreted protein
Target 7 Gene Sequence >738 bp 
ATGGACGTGGGGCCCAGCTCCCTGCCCCACCTTGGGCTGAAGCTGCTGCTGCTCCTGCTG
CTGCTGCCCCTCAGGGCCAAAGCCAACACAGGCTGCTACGGGATCCCAGGGATGCCCGGC
CTGCCCGGGGCACCAGGGAAGGATGGGTACGACGGACTGCCGGGGCCCAAGGGGGAGCCA
GGAATCCCAGCCATTCCCGGGATCCGAGGACCCAAAGGGCAGAAGGGAGAACCCGGCTTA
CCCGGCCATCCTGGGAAAAATGGCCCCATGGGACCCCCTGGGATGCCAGGGGTGCCCGGC
CCCATGGGATTCCCTGGAGAGCCAGGTGAGGAGGGCAGATACAAGCAGAAATTCCAGTCA
GTGTTCACGGTCACTCGGCAGACCCACCAGCCCCCTGCACCCAACAGCCTGATCAGATTC
AACGCGGTCCTCACCAACCCGCAGGAGGATTATGACACGAGCACTGGCAAGTTCACCTGC
AAAGTCCCCGGCCTCTACTACTTTGTCTACCACGCGTCGCATACAGCCAACCTGTGCGTG
CTGCTGTACCGCAGCGGCGTCAAAGTGGTCACCTTCTGTGGCCACACGTCCAAAACCAAT
CAGGTCAACTCGGGCGGTGTGCTGCTGAGGTTGCAGGTGGGCGAGGAGGTGTGGCTGGCT
GTCAATGACTACTACGACATGGTGGGCATCCAGGGCTCTGACAGCGTCTTCTCCGGCTTC
CTGCTCTTCCCCGACTAG
Target 7 GenBank Gene ID
Target 7 GeneCard ID C1QC Link Image
Target 7 GenAtlas ID C1QC Link Image
Target 7 HGNC ID HGNC:1245 Link Image
Target 7 Chromosome Location 1
Target 7 Locus 1p36.11
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. Petry F: Molecular basis of hereditary C1q deficiency. Immunobiology. 1998 Aug;199(2):286-94. [PubMed Link Image]
Target 7 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 3818
Target 8 Name Low affinity immunoglobulin gamma Fc region receptor III-A
Target 8 Synonyms
  1. CD16a antigen
  2. Fc-gamma RIII
  3. Fc-gamma RIII-alpha
  4. Fc-gamma RIIIa
  5. FcR-10
  6. FcRIII
  7. FcRIIIa
  8. IgG Fc receptor III-2
  9. Low affinity immunoglobulin gamma Fc region receptor III-A precursor
Target 8 Gene Name FCGR3A
Target 8 Protein Sequence >Low affinity immunoglobulin gamma Fc region receptor III-A 
MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQW
FHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKE
EDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKN
VSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDW
KDHKFKWRKDPQDK
Target 8 Number of Residues 258
Target 8 Molecular Weight 29089
Target 8 Theoretical pI 8.21
Target 8 GO Classification Not Available
Target 8 General Function Not Available
Target 8 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
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • 1-16
Target 8 Transmembrane Regions
  • 209-229
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 31324 Link Image
Target 8 UniProtKB/Swiss-Prot ID P08637 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name FCG3A_HUMAN Link Image
Target 8 PDB ID 1E4K Link Image
Target 8 PDB File Show
Target 8 3D Structure
Target 8 Cellular Location
  • Cell membrane
Target 8 Gene Sequence >765 bp 
ATGTGGCAGCTGCTCCTCCCAACTGCTCTGCTACTTCTAGTTTCAGCTGGCATGCGGACT
GAAGATCTCCCAAAGGCTGTGGTGTTCCTGGAGCCTCAATGGTACAGGGTGCTCGAGAAG
GACAGTGTGACTCTGAAGTGCCAGGGAGCCTACTCCCCTGAGGACAATTCCACACAGTGG
TTTCACAATGAGAGCCTCATCTCAAGCCAGGCCTCGAGCTACTTCATTGACGCTGCCACA
GTCGACGACAGTGGAGAGTACAGGTGCCAGACAAACCTCTCCACCCTCAGTGACCCGGTG
CAGCTAGAAGTCCATATCGGCTGGCTGTTGCTCCAGGCCCCTCGGTGGGTGTTCAAGGAG
GAAGACCCTATTCACCTGAGGTGTCACAGCTGGAAGAACACTGCTCTGCATAAGGTCACA
TATTTACAGAATGGCAAAGGCAGGAAGTATTTTCATCATAATTCTGACTTCTACATTCCA
AAAGCCACACTCAAAGACAGCGGCTCCTACTTCTGCAGGGGGCTTTTTGGGAGTAAAAAT
GTGTCTTCAGAGACTGTGAACATCACCATCACTCAAGGTTTGGCAGTGTCAACCATCTCA
TCATTCTTTCCACCTGGGTACCAAGTCTCTTTCTGCTTGGTGATGGTACTCCTTTTTGCA
GTGGACACAGGACTATATTTCTCTGTGAAGACAAACATTCGAAGCTCAACAAGAGACTGG
AAGGACCATAAATTTAAATGGAGAAAGGACCCTCAAGACAAATGA
Target 8 GenBank Gene ID
Target 8 GeneCard ID FCGR3A Link Image
Target 8 GenAtlas ID FCGR3A Link Image
Target 8 HGNC ID HGNC:3619 Link Image
Target 8 Chromosome Location 1
Target 8 Locus 1q23
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
Target 8 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 9 [top]
Target 9 ID 3819
Target 9 Name Low affinity immunoglobulin gamma Fc region receptor II-a
Target 9 Synonyms
  1. CD32 antigen
  2. CDw32
  3. Fc-gamma RII-a
  4. Fc-gamma-RIIa
  5. FcRII-a
  6. IgG Fc receptor II-a
  7. Low affinity immunoglobulin gamma Fc region receptor II-a precursor
Target 9 Gene Name FCGR2A
Target 9 Protein Sequence >Low affinity immunoglobulin gamma Fc region receptor II-a 
MAMETQMSQNVCPRNLWLLQPLTVLLLLASADSQAAAPPKAVLKLEPPWINVLQEDSVTL
TCQGARSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSLSDPVHLTVL
SEWLVLQTPHLEFQEGETIMLRCHSWKDKPLVKVTFFQNGKSQKFSRLDPTFSIPQANHS
HSGDYHCTGNIGYTLFSSKPVTITVQVPSMGSSSPMGIIVAVVIATAVAAIVAAVVALIY
CRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQLEETNNDYETADGGYMTLNPRAPTDDD
KNIYLTLPPNDHVNSNN
Target 9 Number of Residues 322
Target 9 Molecular Weight 34990
Target 9 Theoretical pI 6.78
Target 9 GO Classification Not Available
Target 9 General Function Not Available
Target 9 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
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • 1-33
Target 9 Transmembrane Regions
  • 218-240
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 182474 Link Image
Target 9 UniProtKB/Swiss-Prot ID P12318 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name FCG2A_HUMAN Link Image
Target 9 PDB ID 1H9V Link Image
Target 9 PDB File Show
Target 9 3D Structure
Target 9 Cellular Location
  • Membrane
Target 9 Gene Sequence >954 bp 
ATGGCTATGGAGACCCAAATGTCTCAGAATGTATGTCCCAGAAACCTGTGGCTGCTTCAA
CCATTGACAGTTTTGCTGCTGCTGGCTTCTGCAGACAGTCAAGCTGCAGCTCCCCCAAAG
GCTGTGCTGAAACTTGAGCCCCCGTGGATCAACGTGCTCCAGGAGGACTCTGTGACTCTG
ACATGCCAGGGGGCTCGCAGCCCTGAGAGCGACTCCATTCAGTGGTTCCACAATGGGAAT
CTCATTCCCACCCACACGCAGCCCAGCTACAGGTTCAAGGCCAACAACAATGACAGCGGG
GAGTACACGTGCCAGACTGGCCAGACCAGCCTCAGCGACCCTGTGCATCTGACTGTGCTT
TCCGAATGGCTGGTGCTCCAGACCCCTCACCTGGAGTTCCAGGAGGGAGAAACCATCATG
CTGAGGTGCCACAGCTGGAAGGACAAGCCTCTGGTCAAGGTCACATTCTTCCAGAATGGA
AAATCCCAGAAATTCTCCCGTTTGGATCCCACCTTCTCCATCCCACAAGCAAACCACAGT
CACAGTGGTGATTACCACTGCACAGGAAACATAGGCTACACGCTGTTCTCATCCAAGCCT
GTGACCATCACTGTCCAAGTGCCCAGCATGGGCAGCTCTTCACCAATGGGGATCATTGTG
GCTGTGGTCATTGCGACTGCTGTAGCAGCCATTGTTGCTGCTGTAGTGGCCTTGATCTAC
TGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTGAAGGCTGCCCAATTTGAG
CCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACTTGAAGAAACCAACAATGAC
TATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGGGCACCTACTGACGATGAT
AAAAACATCTACCTGACTCTTCCTCCCAACGACCATGTCAACAGTAATAACTAA
Target 9 GenBank Gene ID
Target 9 GeneCard ID FCGR2A Link Image
Target 9 GenAtlas ID FCGR2A Link Image
Target 9 HGNC ID HGNC:3616 Link Image
Target 9 Chromosome Location 1
Target 9 Locus 1q23
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. Seki T: Identification of multiple isoforms of the low-affinity human IgG Fc receptor. Immunogenetics. 1989;30(1):5-12. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
  6. 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. [PubMed Link Image]
  7. 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. [PubMed Link Image]
  8. 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. [PubMed Link Image]
Target 9 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 3820
Target 10 Name Low affinity immunoglobulin gamma Fc region receptor II-b
Target 10 Synonyms
  1. CD32 antigen
  2. CDw32
  3. Fc-gamma RII-b
  4. Fc-gamma-RIIb
  5. FcRII-b
  6. IgG Fc receptor II-b
  7. Low affinity immunoglobulin gamma Fc region receptor II-b precursor
Target 10 Gene Name FCGR2B
Target 10 Protein Sequence >Low affinity immunoglobulin gamma Fc region receptor II-b 
MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN
VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL
SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN
FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA
VVALIYCRKKRISALPGYPECREMGETLPEKPANPTNPDEADKVGAENTITYSLLMHPDA
LEEPDDQNRI
Target 10 Number of Residues 315
Target 10 Molecular Weight 34044
Target 10 Theoretical pI 6.12
Target 10 GO Classification Not Available
Target 10 General Function Not Available
Target 10 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
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function
Target 10 Signals
  • 1-42
Target 10 Transmembrane Regions
  • 218-240
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 4099445 Link Image
Target 10 UniProtKB/Swiss-Prot ID P31994 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name FCG2B_HUMAN Link Image
Target 10 PDB ID 2FCB Link Image
Target 10 PDB File Show
Target 10 3D Structure
Target 10 Cellular Location
  • Membrane
Target 10 Gene Sequence >930 bp 
ATGGGAATCCTGTCATTCTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG
TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT
GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC
GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC
TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG
TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC
AGCGACCCTGTGCATCTGACTGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG
GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG
GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC
TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCACTGCACAGGAAACATA
GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA
CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCGGCCATTGTTGCTGCT
GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCTCTCCCAGGATACCCTGAG
TGCAGGGAAATGGGAGAGACCCTCCCTGAGAAACCAGCCAATCCCACTAATCCTGATGAG
GCTGACAAAGTTGGGGCTGAGAACACAATCACCTATTCACTTCTCATGCACCCGGATGCT
CTGGAAGAGCCTGATGACCAGAACCGTATT
Target 10 GenBank Gene ID
Target 10 GeneCard ID FCGR2B Link Image
Target 10 GenAtlas ID FCGR2B Link Image
Target 10 HGNC ID HGNC:3618 Link Image
Target 10 Chromosome Location 1
Target 10 Locus 1q23
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
Target 10 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]
Drug Target 11 [top]
Target 11 ID 3821
Target 11 Name Low affinity immunoglobulin gamma Fc region receptor II-c
Target 11 Synonyms
  1. CD32 antigen
  2. CDw32
  3. Fc-gamma RII-c
  4. Fc-gamma-RIIc
  5. FcRII-c
  6. IgG Fc receptor II-c
  7. Low affinity immunoglobulin gamma Fc region receptor II-c precursor
Target 11 Gene Name FCGR2C
Target 11 Protein Sequence >Low affinity immunoglobulin gamma Fc region receptor II-c 
MGILSFLPVLATESDWADCKSPQPWGHMLLWTAVLFLAPVAGTPAAPPKAVLKLEPQWIN
VLQEDSVTLTCRGTHSPESDSIQWFHNGNLIPTHTQPSYRFKANNNDSGEYTCQTGQTSL
SDPVHLTVLSEWLVLQTPHLEFQEGETIVLRCHSWKDKPLVKVTFFQNGKSKKFSRSDPN
FSIPQANHSHSGDYHCTGNIGYTLYSSKPVTITVQAPSSSPMGIIVAVVTGIAVAAIVAA
VVALIYCRKKRISANSTDPVKAAQFEPPGRQMIAIRKRQPEETNNDYETADGGYMTLNPR
APTDDDKNIYLTLPPNDHVNSNN
Target 11 Number of Residues 328
Target 11 Molecular Weight 35578
Target 11 Theoretical pI 6.90
Target 11 GO Classification Not Available
Target 11 General Function Not Available
Target 11 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
Target 11 Pathways Not Available
Target 11 Reactions Not Available
Target 11 Pfam Domain Function
Target 11 Signals
  • 1-42
Target 11 Transmembrane Regions
  • 224-246
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 32074 Link Image
Target 11 UniProtKB/Swiss-Prot ID P31995 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name FCG2C_HUMAN Link Image
Target 11 PDB ID 2FCB Link Image
Target 11 PDB File Show
Target 11 3D Structure
Target 11 Cellular Location
  • Cell membrane
Target 11 Gene Sequence >972 bp 
ATGGGAATCCTGTCATTTTTACCTGTCCTTGCCACTGAGAGTGACTGGGCTGACTGCAAG
TCCCCCCAGCCTTGGGGTCATATGCTTCTGTGGACAGCTGTGCTATTCCTGGCTCCTGTT
GCTGGGACACCTGCAGCTCCCCCAAAGGCTGTGCTGAAACTCGAGCCCCAGTGGATCAAC
GTGCTCCAGGAGGACTCTGTGACTCTGACATGCCGGGGGACTCACAGCCCTGAGAGCGAC
TCCATTCAGTGGTTCCACAATGGGAATCTCATTCCCACCCACACGCAGCCCAGCTACAGG
TTCAAGGCCAACAACAATGACAGCGGGGAGTACACGTGCCAGACTGGCCAGACCAGCCTC
AGCGACCCTGTGCATCTGACAGTGCTTTCTGAGTGGCTGGTGCTCCAGACCCCTCACCTG
GAGTTCCAGGAGGGAGAAACCATCGTGCTGAGGTGCCACAGCTGGAAGGACAAGCCTCTG
GTCAAGGTCACATTCTTCCAGAATGGAAAATCCAAGAAATTTTCCCGTTCGGATCCCAAC
TTCTCCATCCCACAAGCAAACCACAGTCACAGTGGTGATTACCATTGCACAGGAAACATA
GGCTACACGCTGTACTCATCCAAGCCTGTGACCATCACTGTCCAAGCTCCCAGCTCTTCA
CCGATGGGGATCATTGTGGCTGTGGTCACTGGGATTGCTGTAGCTGCCATTGTTGCTGCT
GTAGTGGCCTTGATCTACTGCAGGAAAAAGCGGATTTCAGCCAATTCCACTGATCCTGTG
AAGGCTGCCCAATTTGAGCCACCTGGACGTCAAATGATTGCCATCAGAAAGAGACAACCT
GAAGAAACCAACAATGACTATGAAACAGCTGACGGCGGCTACATGACTCTGAACCCCAGG
GCACCTACTGACGATGATAAAAACATCTACTTGACTCTTCCTCCCAACGACCATGTCAAC
AGTAATAACTAA
Target 11 GenBank Gene ID
Target 11 GeneCard ID FCGR2C Link Image
Target 11 GenAtlas ID FCGR2C Link Image
Target 11 HGNC ID HGNC:15626 Link Image
Target 11 Chromosome Location 1
Target 11 Locus 1q23.3
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
Target 11 Drug References
  1. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. [PubMed Link Image]
  2. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. [PubMed Link Image]

This project is supported by Genome Alberta & Genome Canada, a not-for-profit organization that is leading Canada's national genomics strategy with $600 million in funding from the federal government. This project is also supported in part by GenomeQuest, Inc., an enterprise genomic information company serving the life science community.