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Showing drug card for Antihemophilic Factor (DB00025)

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Version 2.5
Creation Date 2005-06-13 13:24:05
Update Date 2009-02-19 16:03:16
Primary Accession Number DB00025
Secondary Accession Number
  • BIOD00029
  • BTD00029
Name Antihemophilic Factor
Drug Type
  • Approved
  • Biotech
  • Investigational
Description Human recombinant antihemophilic factor (AHF) or Factor VIII, 2332 residues, glycosylated, produced by CHO cells
Synonyms
  1. AHF
  2. Coagulation factor VIII precursor
  3. Procoagulant component
  4. antihemophilic factor
Brand Names
  1. Advate
  2. Alphanate
  3. Bioclate
  4. Helixate
  5. Helixate FS
  6. Hemofil M
  7. Humate-P
  8. Hyate:C
  9. Koate-HP
  10. Kogenate
  11. Kogenate FS
  12. Monarc-M
  13. Monoclate-P
  14. ReFacto
  15. Xyntha
Brand Mixtures Not Available
Chemical IUPAC Name Not Available
Chemical Formula C11794H18314N3220O3553S83
Chemical Structure Structure
Protein Sequence(s) >DB00025 sequence
ATRRYYLGAVELSWDYMQSDLGELPVDARFPPRVPKSFPFNTSVVYKKTLFVEFTDHLFN
IAKPRPPWMGLLGPTIQAEVYDTVVITLKNMASHPVSLHAVGVSYWKASEGAEYDDQTSQ
REKEDDKVFPGGSHTYVWQVLKENGPMASDPLCLTYSYLSHVDLVKDLNSGLIGALLVCR
EGSLAKEKTQTLHKFILLFAVFDEGKSWHSETKNSLMQDRDAASARAWPKMHTVNGYVNR
SLPGLIGCHRKSVYWHVIGMGTTPEVHSIFLEGHTFLVRNHRQASLEISPITFLTAQTLL
MDLGQFLLFCHISSHQHDGMEAYVKVDSCPEEPQLRMKNNEEAEDYDDDLTDSEMDVVRF
DDDNSPSFIQIRSVAKKHPKTWVHYIAAEEEDWDYAPLVLAPDDRSYKSQYLNNGPQRIG
RKYKKVRFMAYTDETFKTREAIQHESGILGPLLYGEVGDTLLIIFKNQASRPYNIYPHGI
TDVRPLYSRRLPKGVKHLKDFPILPGEIFKYKWTVTVEDGPTKSDPRCLTRYYSSFVNME
RDLASGLIGPLLICYKESVDQRGNQIMSDKRNVILFSVFDENRSWYLTENIQRFLPNPAG
VQLEDPEFQASNIMHSINGYVFDSLQLSVCLHEVAYWYILSIGAQTDFLSVFFSGYTFKH
KMVYEDTLTLFPFSGETVFMSMENPGLWILGCHNSDFRNRGMTALLKVSSCDKNTGDYYE
DSYEDISAYLLSKNNAIEPRSFSQNSRHPSTRQKQFNATTIPENDIEKTDPWFAHRTPMP
KIQNVSSSDLLMLLRQSPTPHGLSLSDLQEAKYETFSDDPSPGAIDSNNSLSEMTHFRPQ
LHHSGDMVFTPESGLQLRLNEKLGTTAATELKKLDFKVSSTSNNLISTIPSDNLAAGTDN
TSSLGPPSMPVHYDSQLDTTLFGKKSSPLTESGGPLSLSEENNDSKLLESGLMNSQESSW
GKNVSSTESGRLFKGKRAHGPALLTKDNALFKVSISLLKTNKTSNNSATNRKTHIDGPSL
LIENSPSVWQNILESDTEFKKVTPLIHDRMLMDKNATALRLNHMSNKTTSSKNMEMVQQK
KEGPIPPDAQNPDMSFFKMLFLPESARWIQRTHGKNSLNSGQGPSPKQLVSLGPEKSVEG
QNFLSEKNKVVVGKGEFTKDVGLKEMVFPSSRNLFLTNLDNLHENNTHNQEKKIQEEIEK
KETLIQENVVLPQIHTVTGTKNFMKNLFLLSTRQNVEGSYDGAYAPVLQDFRSLNDSTNR
TKKHTAHFSKKGEEENLEGLGNQTKQIVEKYACTTRISPNTSQQNFVTQRSKRALKQFRL
PLEETELEKRIIVDDTSTQWSKNMKHLTPSTLTQIDYNEKEKGAITQSPLSDCLTRSHSI
PQANRSPLPIAKVSSFPSIRPIYLTRVLFQDNSSHLPAASYRKKDSGVQESSHFLQGAKK
NNLSLAILTLEMTGDQREVGSLGTSATNSVTYKKVENTVLPKPDLPKTSGKVELLPKVHI
YQKDLFPTETSNGSPGHLDLVEGSLLQGTEGAIKWNEANRPGKVPFLRVATESSAKTPSK
LLDPLAWDNHYGTQIPKEEWKSQEKSPEKTAFKKKDTILSLNACESNHAIAAINEGQNKP
EIEVTWAKQGRTERLCSQNPPVLKRHQREITRTTLQSDQEEIDYDDTISVEMKKEDFDIY
DEDENQSPRSFQKKTRHYFIAAVERLWDYGMSSSPHVLRNRAQSGSVPQFKKVVFQEFTD
GSFTQPLYRGELNEHLGLLGPYIRAEVEDNIMVTFRNQASRPYSFYSSLISYEEDQRQGA
EPRKNFVKPNETKTYFWKVQHHMAPTKDEFDCKAWAYFSDVDLEKDVHSGLIGPLLVCHT
NTLNPAHGRQVTVQEFALFFTIFDETKSWYFTENMERNCRAPCNIQMEDPTFKENYRFHA
INGYIMDTLPGLVMAQDQRIRWYLLSMGSNENIHSIHFSGHVFTVRKKEEYKMALYNLYP
GVFETVEMLPSKAGIWRVECLIGEHLHAGMSTLFLVYSNKCQTPLGMASGHIRDFQITAS
GQYGQWAPKLARLHYSGSINAWSTKEPFSWIKVDLLAPMIIHGIKTQGARQKFSSLYISQ
FIIMYSLDGKKWQTYRGNSTGTLMVFFGNVDSSGIKHNIFNPPIIARYIRLHPTHYSIRS
TLRMELMGCDLNSCSMPLGMESKAISDAQITASSYFTNMFATWSPSKARLHLQGRSNAWR
PQVNNPKEWLQVDFQKTMKVTGVTTQGVKSLLTSMYVKEFLISSSQDGHQWTLFFQNGKV
KVFQGNQDSFTPVVNSLDPPLLTRYLRIHPQSWVHQIALRMEVLGCEAQDLY
CAS Registry Number Not Available
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 PA448445 Link Image
HET ID Not Available
GenBank ID M14113 Link Image
Drug ID Number [DIN] 02242491 Link Image
RxList Link http://www.rxlist.com/cgi/generic2/hemofilm.htm Link Image
PDRhealth Link Not Available
Wikipedia Link http://en.wikipedia.org/wiki/Antihemophilic_Factor Link Image
FDA Label Not Available
Material Safety Data Sheet (MSDS) Not Available
Synthesis Reference Not Available
Average Molecular Weight 264725.5000
Monoisotopic Molecular Weight Not Available
State Solid
Melting Point Not Available
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility Not Available Calculated using ALOGPS
Experimental LogP/Hydrophobicity -0.533 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 6.97
Mass Spectrum Not Available
MOL File Not Available
SDF File Not Available
PDB File Not Available
Experimental PDB ID 2R7E Link Image
Experimental PDB File Show
Experimental PDB Structure
Isomeric SMILES Not Available
Canonical SMILES Not Available
Drug Category
  • Coagulants
  • Thrombotic Agents
ATC Codes
AHFS Codes
  • 20:28.16
Indication For the treatment of hemophilia A, von Willebrand diseae and Factor XIII deficiency
Pharmacology Antihemophilic Factor binds factor IXa along with calcium and phospholipid, This complex converts factor X to factor Xa to facilitate clotting cascade.
Mechanism of Action Antihemophilic factor (AHF) is a protein found in normal plasma which is necessary for clot formation. The administration of AHF provides an increase in plasma levels of AHF and can temporarily correct the coagulation defect of patients with hemophilia A (classical hemophilia).
Absorption Not Available
Toxicity Not Available
Protein Binding Not Available
Biotransformation Not Available
Half Life 8.4-19.3 hrs
Dosage Forms
Form Route
Powder, for solution Intravenous
Patient Information Not Available
Contraindications Show Link Image
Interactions Not Available
Drug Interactions Not Available
Food Interactions Not Available
Pathways Not Available
General References
  1. Titheradge MA, Coore HG: Initial rates of pyruvate transport in mitochondria determined by an "inhibitor-stop" technique. Biochem J. 1975 Sep;150(3):553-6. [PubMed Link Image]
  2. Drugs.com Link Image
  3. Wikipedia Link Image
  4. RxList Link Image
Organisms Affected
  • Humans and other mammals
Phase 1 Metabolizing Enzymes
  1. Cytochrome P450 2C9 (CYP2C9)
Targets
  1. Prothrombin
  2. Coagulation factor X
  3. Coagulation factor IX
  4. Vitamin K-dependent protein C
  5. Vitamin K-dependent protein S
  6. Calnexin
  7. von Willebrand factor
  8. 78 kDa glucose-regulated protein
  9. Calreticulin
  10. Low-density lipoprotein receptor-related protein 1
  11. Phytanoyl-CoA dioxygenase, peroxisomal
  12. Asialoglycoprotein receptor 2
  13. ERGIC-53 protein
  14. Multiple coagulation factor deficiency protein 2
Phase 1 Metabolizing Enzyme 1 [top]
Enzyme 1 Name Cytochrome P450 2C9 (CYP2C9)
Enzyme 1 Gene Name CYP2C9
Enzyme 1 SwissProt ID P11712 Link Image
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 Protein Sequence >sp|P11712|CP2C9_HUMAN Cytochrome P450 2C9 (EC 1.14.13.80)
MDSLVVLVLCLSCLLLLSLWRQSSGRGKLPPGPTPLPVIGNILQIGIKDISKSLTNLSKV
YGPVFTLYFGLKPIVVLHGYEAVKEALIDLGEEFSGRGIFPLAERANRGFGIVFSNGKKW
KEIRRFSLMTLRNFGMGKRSIEDRVQEEARCLVEELRKTKASPCDPTFILGCAPCNVICS
IIFHKRFDYKDQQFLNLMEKLNENIKILSSPWIQICNNFSPIIDYFPGTHNKLLKNVAFM
KSYILEKVKEHQESMDMNNPQDFIDCFLMKMEKEKHNQPSEFTIESLENTAVDLFGAGTE
TTSTTLRYALLLLLKHPEVTAKVQEEIERVIGRNRSPCMQDRSHMPYTDAVVHEVQRYID
LLPTSLPHAVTCDIKFRNYLIPKGTTILISLTSVLHDNKEFPNPEMFDPHHFLDEGGNFK
KSKYFMPFSAGKRICVGEALAGMELFLFLTSILQNFNLKSLVDPKNLDTTPVVNGFASVP
PFYQLCFIPV
Drug Target 1 [top]
Target 1 ID 54
Target 1 Name Prothrombin
Target 1 Synonyms
  1. Activated Factor II [IIa]
  2. Coagulation factor II
  3. EC 3.4.21.5
  4. Prothrombin precursor
  5. Thrombin
Target 1 Gene Name F2
Target 1 Protein Sequence >Prothrombin precursor
MAHVRGLQLPGCLALAALCSLVHSQHVFLAPQQARSLLQRVRRANTFLEEVRKGNLEREC
VEETCSYEEAFEALESSTATDVFWAKYTACETARTPRDKLAACLEGNCAEGLGTNYRGHV
NITRSGIECQLWRSRYPHKPEINSTTHPGADLQENFCRNPDSSTTGPWCYTTDPTVRRQE
CSIPVCGQDQVTVAMTPRSEGSSVNLSPPLEQCVPDRGQQYQGRLAVTTHGLPCLAWASA
QAKALSKHQDFNSAVQLVENFCRNPDGDEEGVWCYVAGKPGDFGYCDLNYCEEAVEEETG
DGLDEDSDRAIEGRTATSEYQTFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYI
DGRIVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTEN
DLLVRIGKHSRTRYERNIEKISMLEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHP
VCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVLQVVNLPIVERPVCKDST
RIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKY
GFYTHVFRLKKWIQKVIDQFGE
Target 1 Number of Residues 632
Target 1 Molecular Weight 70037
Target 1 Theoretical pI 5.70
Target 1 GO Classification
Function
thrombin activity
binding
ion binding
cation binding
calcium ion binding
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
Process
organismal physiological process
regulation of body fluids
hemostasis
blood coagulation
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
Component
extracellular region
Target 1 General Function Involved in blood clotting cascade
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
Target 1 Pathways Not Available
Target 1 Reactions
  • 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
Target 1 Pfam Domain Function
Target 1 Signals
  • 1-24
Target 1 Transmembrane Regions
  • None
Target 1 Essentiality Non-Essential
Target 1 GenBank ID Protein 339641 Link Image
Target 1 UniProtKB/Swiss-Prot ID P00734 Link Image
Target 1 UniProtKB/Swiss-Prot Entry Name THRB_HUMAN Link Image
Target 1 PDB ID 1HAG Link Image
Target 1 PDB File Show
Target 1 3D Structure
Target 1 Cellular Location
  • Secreted protein
  • extracellular space
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
Target 1 GenBank Gene ID
Target 1 GeneCard ID F2 Link Image
Target 1 GenAtlas ID F2 Link Image
Target 1 HGNC ID HGNC:3535 Link Image
Target 1 Chromosome Location 11
Target 1 Locus 11p11-q12
Target 1 SNPs SNPJam Report Link Image
Target 1 General References
  1. 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. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. 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. [PubMed Link Image]
  4. 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. [PubMed Link Image]
  5. 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. [PubMed Link Image]
  6. 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. [PubMed Link Image]
  7. 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. [PubMed Link Image]
  8. 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. [PubMed Link Image]
  9. 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. [PubMed Link Image]
  10. Degen SJ, Davie EW: Nucleotide sequence of the gene for human prothrombin. Biochemistry. 1987 Sep 22;26(19):6165-77. [PubMed Link Image]
  11. 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.
  12. 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.
  13. 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.
  14. 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.
  15. 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.
  16. 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.
  17. 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.
  18. 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.
  19. 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.
  20. 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.
  21. 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.
  22. 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.
Target 1 Drug References
  1. Alberio L, Safa O, Clemetson KJ, Esmon CT, Dale GL: Surface expression and functional characterization of alpha-granule factor V in human platelets: effects of ionophore A23187, thrombin, collagen, and convulxin. Blood. 2000 Mar 1;95(5):1694-702. [PubMed Link Image]
  2. Ratnoff OD, Lewis JH: Heckathorn's disease: variable functional dificiency of antihemophilic factor (factor VIII). Blood. 1975 Aug;46(2):161-73. [PubMed Link Image]
  3. Anderson DM, Shelley S, Crick N, Buraglio M: No effect of the novel antidiabetic agent nateglinide on the pharmacokinetics and anticoagulant properties of warfarin in healthy volunteers. J Clin Pharmacol. 2002 Dec;42(12):1358-65. [PubMed Link Image]
  4. Piet MP, Chin S, Prince AM, Brotman B, Cundell AM, Horowitz B: The use of tri(n-butyl)phosphate detergent mixtures to inactivate hepatitis viruses and human immunodeficiency virus in plasma and plasma's subsequent fractionation. Transfusion. 1990 Sep;30(7):591-8. [PubMed Link Image]
  5. Lazarchick J, Ashby MA, Lazarchick JJ, Sens DA: Mechanism of factor VIII inactivation by human antibodies. IV. Antibody binding prevents factor VIII proteolysis by thrombin. Ann Clin Lab Sci. 1986 Nov-Dec;16(6):497-501. [PubMed Link Image]
Drug Target 2 [top]
Target 2 ID 239
Target 2 Name Coagulation factor X
Target 2 Synonyms
  1. Coagulation factor X precursor
  2. EC 3.4.21.6
  3. Stuart factor
  4. Stuart- Prower factor
Target 2 Gene Name F10
Target 2 Protein Sequence >Coagulation factor X precursor
MGRPLHLVLLSASLAGLLLLGESLFIRREQANNILARVTRANSFLEEMKKGHLERECMEE
TCSYEEAREVFEDSDKTNEFWNKYKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKN
CELFTRKLCSLDNGDCDQFCHEEQNSVVCSCARGYTLADNGKACIPTGPYPCGKQTLERR
KRSVAQATSSSGEAPDSITWKPYDAADLDPTENPFDLLDFNQTQPERGDNNLTRIVGGQE
CKDGECPWQALLINEENEGFCGGTILSEFYILTAAHCLYQAKRFKVRVGDRNTEQEEGGE
AVHEVEVVIKHNRFTKETYDFDIAVLRLKTPITFRMNVAPACLPERDWAESTLMTQKTGI
VSGFGRTHEKGRQSTRLKMLEVPYVDRNSCKLSSSFIITQNMFCAGYDTKQEDACQGDSG
GPHVTRFKDTYFVTGIVSWGEGCARKGKYGIYTKVTAFLKWIDRSMKTRGLPKAKSHAPE
VITSSPLK
Target 2 Number of Residues 496
Target 2 Molecular Weight 54732
Target 2 Theoretical pI 5.74
Target 2 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
binding
ion binding
cation binding
calcium ion binding
Process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
physiological process
organismal physiological process
regulation of body fluids
hemostasis
blood coagulation
Component
extracellular region
Target 2 General Function Involved in calcium ion binding
Target 2 Specific Function Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting
Target 2 Pathways Not Available
Target 2 Reactions
  • Selective cleavage of Arg!Thr and then Arg!Ile bonds in prothrombin to form thrombin
Target 2 Pfam Domain Function
Target 2 Signals
  • 1-31
Target 2 Transmembrane Regions
  • 7-26
Target 2 Essentiality Non-Essential
Target 2 GenBank ID Protein 182841 Link Image
Target 2 UniProtKB/Swiss-Prot ID P00742 Link Image
Target 2 UniProtKB/Swiss-Prot Entry Name FA10_HUMAN Link Image
Target 2 PDB ID 1P0S Link Image
Target 2 PDB File Show
Target 2 3D Structure
Target 2 Cellular Location
  • Cytoplasmic
Target 2 Gene Sequence >1433 bp
CCTCCCTGGCTGGCCTCCTGCTGCTCGGGGAAAGTCTGTTCATCCGCAGGGAGCAGGCCA
ACAACATCCTGGCGAGGGTCACGAGGGCCAATTCCTTTCTTGAAGAGATGAAGAAAGGAC
ACCTCGAAAGAGAGTGCATGGAAGAGACCTGCTCATACGAAGAGGCCCGCGAGGTCTTTG
AGGACAGCGACAAGACGAATGAATTCTGGAATAAATACAAAGATGGCGACCAGTGTGAGA
CCAGTCCTTGCCAGAACCAGGGCAAATGTAAAGACGGCCTCGGGGAATACACCTGCACCT
GTTTAGAAGGATTCGAAGGCAAAAACTGTGAATTATTCACACGGAAGCTCTGCAGCCTGG
ACAACGGGGACTGTGACCAGTTCTGCCACGAGGAACAGAACTCTGTGGTGTGCTCCTGCG
CCCGCGGGTACACCCTGGCTGACAACGGCAAGGCCTGCATTCCCACAGGGCCCTACCCCT
GTGGGAAACAGACCCTGGAACGCAGGAAGAGGTCAGTGGCCCAGGCCACCAGCAGCAGCG
GGGAGGCCCCTGACAGCATCACATGGAAGCCATATGATGCAGCCGACCTGGACCCCACCG
AGAACCCCTTCGACCTGCTTGACTTCAACCAGACGCAGCCTGAGAGGGGCGACAACAACC
TCACCAGGATCGTGGGAGGCCAGGAATGCAAGGACGGGGAGTGTCCCTGGCAGGCCCTGC
TCATCAATGAGGAAAACGAGGGTTTCTGTGGTGGAACTATTCTGAGCGAGTTCTACATCC
TAACGGCAGCCCACTGTCTCTACCAAGCCAAGAGATTCAAGGTGAGGGTAGGGGACCGGA
ACACGGAGCAGGAGGAGGGCGGTGAGGCGGTGCACGAGGTGGAGGTGGTCATCAAGCACA
ACCGGTTCACAAAGGAGACCTATGACTTCGACATCGCCGTGCTCCGGCTCAAGACCCCCA
TCACCTTCCGCATGAACGTGGCGCCTGCCTGCCTCCCCGAGCGTGACTGGGCCGAGTCCA
CGCTGATGACGCAGAAGACGGGGATTGTGAGCGGCTTCGGGCGCACCCACGAGAAGGGCC
GGCAGTCCACCAGGCTCAAGATGCTGGAGGTGCCCTACGTGGACCGCAACAGCTGCAAGC
TGTCCAGCAGCTTCATCATCACCCAGAACATGTTCTGTGCCGGCTACGACACCAAGCAGG
AGGATGCCTGCCAGGGGGACAGCGGGGGCCCGCACGTCACCCGCTTCAAGGACACCTACT
TCGTGACAGGCATCGTCAGCTGGGGAGAGAGCTGTGCCCGTAAGGGGAAGTACGGGATCT
ACACCAAGGTCACCGCCTTCCTCAAGTGGATCGACAGGTCCATGAAAACCAGGGGCTTGC
CCAAGGCCAAGAGCCATGCCCCGGAGGTCATAACGTCCTCTCCATTAAAGTGA
Target 2 GenBank Gene ID
Target 2 GeneCard ID F10 Link Image
Target 2 GenAtlas ID F10 Link Image
Target 2 HGNC ID HGNC:3528 Link Image
Target 2 Chromosome Location 13
Target 2 Locus 13q34
Target 2 SNPs SNPJam Report Link Image
Target 2 General References
  1. 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. [PubMed Link Image]
  2. Messier TL, Pittman DD, Long GL, Kaufman RJ, Church WR: Cloning and expression in COS-1 cells of a full-length cDNA encoding human coagulation factor X. Gene. 1991 Mar 15;99(2):291-4. [PubMed Link Image]
  3. Fung MR, Hay CW, MacGillivray RT: Characterization of an almost full-length cDNA coding for human blood coagulation factor X. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3591-5. [PubMed Link Image]
  4. Jagadeeswaran P, Reddy SV, Rao KJ, Hamsabhushanam K, Lyman G: Cloning and characterization of the 5' end (exon 1) of the gene encoding human factor X. Gene. 1989 Dec 14;84(2):517-9. [PubMed Link Image]
  5. Kaul RK, Hildebrand B, Roberts S, Jagadeeswaran P: Isolation and characterization of human blood-coagulation factor X cDNA. Gene. 1986;41(2-3):311-4. [PubMed Link Image]
  6. Leytus SP, Foster DC, Kurachi K, Davie EW: Gene for human factor X: a blood coagulation factor whose gene organization is essentially identical with that of factor IX and protein C. Biochemistry. 1986 Sep 9;25(18):5098-102. [PubMed Link Image]
  7. Leytus SP, Chung DW, Kisiel W, Kurachi K, Davie EW: Characterization of a cDNA coding for human factor X. Proc Natl Acad Sci U S A. 1984 Jun;81(12):3699-702. [PubMed Link Image]
  8. McMullen BA, Fujikawa K, Kisiel W, Sasagawa T, Howald WN, Kwa EY, Weinstein B: Complete amino acid sequence of the light chain of human blood coagulation factor X: evidence for identification of residue 63 as beta-hydroxyaspartic acid. Biochemistry. 1983 Jun 7;22(12):2875-84. [PubMed Link Image]
  9. Inoue K, Morita T: Identification of O-linked oligosaccharide chains in the activation peptides of blood coagulation factor X. The role of the carbohydrate moieties in the activation of factor X. Eur J Biochem. 1993 Nov 15;218(1):153-63. [PubMed Link Image]
  10. Padmanabhan K, Padmanabhan KP, Tulinsky A, Park CH, Bode W, Huber R, Blankenship DT, Cardin AD, Kisiel W: Structure of human des(1-45) factor Xa at 2.2 A resolution. J Mol Biol. 1993 Aug 5;232(3):947-66. [PubMed Link Image]
  11. 9618463 Kamata K, Kawamoto H, Honma T, Iwama T, Kim SH: Structural basis for chemical inhibition of human blood coagulation factor Xa. Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6630-5.
Target 2 Drug References
  1. Freedman J, Mody M, Lazarus AH, Dewar L, Song S, Blanchette VS, Garvey MB, Ofosu FA: Platelet activation and hypercoagulability following treatment with porcine factor VIII (HYATE:C). Am J Hematol. 2002 Mar;69(3):192-9. [PubMed Link Image]
  2. BLATRIX C, SOULIER JP: [Preparation of a fraction rich in prothrombin, proconvertin, Stuart factor and antihemophilic factor B (P.P.B. fraction)] Pathol Biol (Paris). 1959 Dec;7:2477-86. [PubMed Link Image]
  3. LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF STUART FACTOR (FACTOR X) BY ACTIVATED ANTIHEMOPHILIC FACTOR (ACTIVATED FACTOR 8). Biochemistry. 1965 Jan;4:113-20. [PubMed Link Image]
  4. Radnoff OD, Saito H: Inhibition of Hageman factor, plasma thromboplastin antecedent, thrombin and other clotting factors by phenylglyoxal hydrate (38500). Proc Soc Exp Biol Med. 1975 Jan;148(1):177-82. [PubMed Link Image]
  5. Orthner CL: Characterization of proteases in AHF concentrates: effect on factor VIII:von Willebrand protein as assessed by high-pressure gel permeation chromatography. J Lab Clin Med. 1984 Nov;104(5):816-28. [PubMed Link Image]
Drug Target 3 [top]
Target 3 ID 400
Target 3 Name Coagulation factor IX
Target 3 Synonyms
  1. Christmas factor
  2. Coagulation factor IX precursor
  3. EC 3.4.21.22
  4. PTC
  5. Plasma thromboplastin component
Target 3 Gene Name F9
Target 3 Protein Sequence >Coagulation factor IX precursor
MQRVNMIMAESPGLITICLLGYLLSAECTVFLDHENANKILNRPKRYNSGKLEEFVQGNL
ERECMEEKCSFEEAREVFENTERTTEFWKQYVDGDQCESNPCLNGGSCKDDINSYECWCP
FGFEGKNCELDVTCNIKNGRCEQFCKNSADNKVVCSCTEGYRLAENQKSCEPAVPFPCGR
VSVSQTSKLTRAETVFPDVDYVNSTEAETILDNITQSTQSFNDFTRVVGGEDAKPGQFPW
QVVLNGKVDAFCGGSIVNEKWIVTAAHCVETGVKITVVAGEHNIEETEHTEQKRNVIRII
PHHNYNAAINKYNHDIALLELDEPLVLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVF
HKGRSALVLQYLRVPLVDRATCLRSTKFTIYNNMFCAGFHEGGRDSCQGDSGGPHVTEVE
GTSFLTGIISWGEECAMKGKYGIYTKVSRYVNWIKEKTKLT
Target 3 Number of Residues 468
Target 3 Molecular Weight 51779
Target 3 Theoretical pI 5.16
Target 3 GO Classification
Function
catalytic activity
hydrolase activity
peptidase activity
endopeptidase activity
serine-type endopeptidase activity
binding
ion binding
cation binding
calcium ion binding
Process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
physiological process
organismal physiological process
regulation of body fluids
hemostasis
blood coagulation
Component
extracellular region
Target 3 General Function Involved in calcium ion binding
Target 3 Specific Function Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa
Target 3 Pathways Not Available
Target 3 Reactions
  • Selective cleavage of Arg!Ile bond in factor X to form factor Xa
Target 3 Pfam Domain Function
Target 3 Signals
  • 1-28
Target 3 Transmembrane Regions
  • None
Target 3 Essentiality Non-Essential
Target 3 GenBank ID Protein 182609 Link Image
Target 3 UniProtKB/Swiss-Prot ID P00740 Link Image
Target 3 UniProtKB/Swiss-Prot Entry Name FA9_HUMAN Link Image
Target 3 PDB ID 1RFN Link Image
Target 3 PDB File Show
Target 3 3D Structure
Target 3 Cellular Location
  • Secreted protein
Target 3 Gene Sequence >1389 bp
ATGCAGCGCGTGAACATGATCATGGCAGAATCACCAAGCCTCATCACCATCTGCCTTTTA
GGATATCTACTCAGTGCTGAATGTACAGTTTTTCTTGATCATGAAAACGCCAACAAAATT
CTGAATCGGCCAAAGAGGTATAATTCAGGTAAATTGGAAGAGTTTGTTCAAGGGAACCTT
GAGAGAGAATGTATGGAAGAAAAGTGTAGTTTTGAAGAACCACGAGAAGTTTTTGAAAAC
ACTGAAAAGACAACTGAATTTTGGAAGCAGTATGTTGATGGAGATCAGTGTGAGTCCAAT
CCATGTTTAAATGGCGGCAGTTGCAAGGATGACATTAATTCCTATGAATGTTGGTGTCCC
TTTGGATTTGAAGGAAAGAACTGTGAATTAGATGTAACATGTAACATTAAGAATGGCAGA
TGCGAGCAGTTTTGTAAAAATAGTGCTGATAACAAGGTGGTTTGCTCCTGTACTGAGGGA
TATCGACTTGCAGAAAACCAGAAGTCCTGTGAACCAGCAGTGCCATTTCCATGTGGAAGA
GTTTCTGTTTCACAAACTTCTAAGCTCACCCGTGCTGAGGCTGTTTTTCCTGATGTGGAC
TATGTAAATCCTACTGAAGCTGAAACCATTTTGGATAACATCACTCAAGGCACCCAATCA
TTTAATGACTTCACTCGGGTTGTTGGTGGAGAAGATGCCAAACCAGGTCAATTCCCTTGG
CAGGTTGTTTTGAATGGTAAAGTTGATGCATTCTGTGGAGGCTCTATCGTTAATGAAAAA
TGGATTGTAACTGCTGCCCACTGTGTTGAAACTGGTGTTAAAATTACAGTTGTCGCAGGT
GAACATAATATTGAGGAGACAGAACATACAGAGCAAAAGCGAAATGTGATTCGAGCAATT
ATTCCTCACCACAACTACAATGCAGCTATTAATAAGTACAACCATGACATTGCCCTTCTG
GAACTGGACGAACCCTTAGTGCTAAACAGCTACGTTACACCTATTTGCATTGCTGACAAG
GAATACACGAACATCTTCCTCAAATTTGGATCTGGCTATGTAAGTGGCTGGGCAAGAGTC
TTCCACAAAGGGAGATCAGCTTTAGTTCTTCAGTACCTTAGAGTTCCACTTGTTGACCGA
GCCACATGTCTTCGATCTACAAAGTTCACCATCTATAACAACATGTTCTGTGCTGGCTTC
CATGAAGGAGGTAGAGATTCATGTCAAGGAGATAGTGGGGGACCCCATGTTACTGAAGTG
GAAGGGACCAGTTTCTTAACTGGAATTATTAGCTGGGGTGAAGAGTGTGCAATGAAAGGC
AAATATGGAATATATACCAAGGTATCCCGGTATGTCAACTGGATTAAGGAAAAAACAAAG
CTCACTTAA
Target 3 GenBank Gene ID
Target 3 GeneCard ID F9 Link Image
Target 3 GenAtlas ID F9 Link Image
Target 3 HGNC ID HGNC:3551 Link Image
Target 3 Chromosome Location X
Target 3 Locus Xq27.1-q27.2
Target 3 SNPs SNPJam Report Link Image
Target 3 General References
  1. Montejo JM, Magallon M, Tizzano E, Solera J: Identification of twenty-one new mutations in the factor IX gene by SSCP analysis. Hum Mutat. 1999;13(2):160-5. [PubMed Link Image]
  2. 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. [PubMed Link Image]
  3. Hopfner KP, Lang A, Karcher A, Sichler K, Kopetzki E, Brandstetter H, Huber R, Bode W, Engh RA: Coagulation factor IXa: the relaxed conformation of Tyr99 blocks substrate binding. Structure. 1999 Aug 15;7(8):989-96. [PubMed Link Image]
  4. Wulff K, Bykowska K, Lopaciuk S, Herrmann FH: Molecular analysis of hemophilia B in Poland: 12 novel mutations of the factor IX gene. Acta Biochim Pol. 1999;46(3):721-6. [PubMed Link Image]
  5. Vidal F, Farssac E, Altisent C, Puig L, Gallardo D: Factor IX gene sequencing by a simple and sensitive 15-hour procedure for haemophilia B diagnosis: identification of two novel mutations. Br J Haematol. 2000 Nov;111(2):549-51. [PubMed Link Image]
  6. Arruda VR, Hagstrom JN, Deitch J, Heiman-Patterson T, Camire RM, Chu K, Fields PA, Herzog RW, Couto LB, Larson PJ, High KA: Posttranslational modifications of recombinant myotube-synthesized human factor IX. Blood. 2001 Jan 1;97(1):130-8. [PubMed Link Image]
  7. Onay UV, Kavakli K, Kilinc Y, Gurgey A, Aktuglu G, Kemahli S, Ozbek U, Caglayan SH: Molecular pathology of haemophilia B in Turkish patients: identification of a large deletion and 33 independent point mutations. Br J Haematol. 2003 Feb;120(4):656-9. [PubMed Link Image]
  8. Espinos C, Casana P, Haya S, Cid AR, Aznar JA: Molecular analyses in hemophilia B families: identification of six new mutations in the factor IX gene. Haematologica. 2003 Feb;88(2):235-6. [PubMed Link Image]
  9. Baron M, Norman DG, Harvey TS, Handford PA, Mayhew M, Tse AG, Brownlee GG, Campbell ID: The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha. Protein Sci. 1992 Jan;1(1):81-90. [PubMed Link Image]
  10. Ludwig M, Sabharwal AK, Brackmann HH, Olek K, Smith KJ, Birktoft JJ, Bajaj SP: Hemophilia B caused by five different nondeletion mutations in the protease domain of factor IX. Blood. 1992 Mar 1;79(5):1225-32. [PubMed Link Image]
  11. 1517205 Nishimura H, Takao T, Hase S, Shimonishi Y, Iwanaga S: Human factor IX has a tetrasaccharide O-glycosidically linked to serine 61 through the fucose residue. J Biol Chem. 1992 Sep 5;267(25):17520-5.
  12. 1615485 Taylor SA, Duffin J, Cameron C, Teitel J, Garvey B, Lillicrap DP: Characterization of the original Christmas disease mutation (cysteine 206----serine): from clinical recognition to molecular pathogenesis. Thromb Haemost. 1992 Jan 23;67(1):63-5.
  13. 1634040 Sommer SS: Assessing the underlying pattern of human germline mutations: lessons from the factor IX gene. FASEB J. 1992 Jul;6(10):2767-74.
  14. 1854745 Huang LH, Cheng H, Pardi A, Tam JP, Sweeney WV: Sequence-specific 1H NMR assignments, secondary structure, and location of the calcium binding site in the first epidermal growth factor like domain of blood coagulation factor IX. Biochemistry. 1991 Jul 30;30(30):7402-9.
  15. 1902289 Sarkar G, Cassady JD, Pyeritz RE, Gilchrist GS, Sommer SS: Isoleucine397 is changed to threonine in two females with hemophilia B. Nucleic Acids Res. 1991 Mar 11;19(5):1165.
  16. 1958666 Miyata T, Sakai T, Sugimoto M, Naka H, Yamamoto K, Yoshioka A, Fukui H, Mitsui K, Kamiya K, Umeyama H, et al.: Factor IX Amagasaki: a new mutation in the catalytic domain resulting in the loss of both coagulant and esterase activities. Biochemistry. 1991 Nov 26;30(47):11286-91.
  17. 2129367 Iwanaga S, Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T: A new trisaccharide sugar chain linked to a serine residue in the first EGF-like domain of clotting factors VII and IX and protein Z. Adv Exp Med Biol. 1990;281:121-31.
  18. 2162822 Bertina RM, van der Linden IK, Mannucci PM, Reinalda-Poot HH, Cupers R, Poort SR, Reitsma PH: Mutations in hemophilia Bm occur at the Arg180-Val activation site or in the catalytic domain of factor IX. J Biol Chem. 1990 Jul 5;265(19):10876-83.
  19. 2339358 Wang NS, Zhang M, Thompson AR, Chen SH: Factor IX Chongqing: a new mutation in the calcium-binding domain of factor IX resulting in severe hemophilia B. Thromb Haemost. 1990 Feb 19;63(1):24-6.
  20. 2372509 Taylor SA, Liddell MB, Peake IR, Bloom AL, Lillicrap DP: A mutation adjacent to the beta cleavage site of factor IX (valine 182 to leucine) results in mild haemophilia Bm. Br J Haematol. 1990 Jun;75(2):217-21.
  21. 2472424 Chen SH, Thompson AR, Zhang M, Scott CR: Three point mutations in the factor IX genes of five hemophilia B patients. Identification strategy using localization by altered epitopes in their hemophilic proteins. J Clin Invest. 1989 Jul;84(1):113-8.
  22. 2511201 Nishimura H, Kawabata S, Kisiel W, Hase S, Ikenaka T, Takao T, Shimonishi Y, Iwanaga S: Identification of a disaccharide (Xyl-Glc) and a trisaccharide (Xyl2-Glc) O-glycosidically linked to a serine residue in the first epidermal growth factor-like domain of human factors VII and IX and protein Z and bovine protein Z. J Biol Chem. 1989 Dec 5;264(34):20320-5.
  23. 2592373 Suehiro K, Kawabata S, Miyata T, Takeya H, Takamatsu J, Ogata K, Kamiya T, Saito H, Niho Y, Iwanaga S: Blood clotting factor IX BM Nagoya. Substitution of arginine 180 by tryptophan and its activation by alpha-chymotrypsin and rat mast cell chymase. J Biol Chem. 1989 Dec 15;264(35):21257-65.
  24. 2713493 Monroe DM, McCord DM, Huang MN, High KA, Lundblad RL, Kasper CK, Roberts HR: Functional consequences of an arginine180 to glutamine mutation in factor IX Hilo. Blood. 1989 May 1;73(6):1540-4.
  25. 2714791 Attree O, Vidaud D, Vidaud M, Amselem S, Lavergne JM, Goossens M: Mutations in the catalytic domain of human coagulation factor IX: rapid characterization by direct genomic sequencing of DNA fragments displaying an altered melting behavior. Genomics. 1989 Apr;4(3):266-72.
  26. 2738071 Ware J, Diuguid DL, Liebman HA, Rabiet MJ, Kasper CK, Furie BC, Furie B, Stafford DW: Factor IX San Dimas. Substitution of glutamine for Arg-4 in the propeptide leads to incomplete gamma-carboxylation and altered phospholipid binding properties. J Biol Chem. 1989 Jul 5;264(19):11401-6.
  27. 2743975 Green PM, Bentley DR, Mibashan RS, Nilsson IM, Giannelli F: Molecular pathology of haemophilia B. EMBO J. 1989 Apr;8(4):1067-72.
  28. 2753873 Sakai T, Yoshioka A, Yamamoto K, Niinomi K, Fujimura Y, Fukui H, Miyata T, Iwanaga S: Blood clotting factor IX Kashihara: amino acid substitution of valine-182 by phenylalanine. J Biochem (Tokyo). 1989 May;105(5):756-9.
  29. 2773937 Koeberl DD, Bottema CD, Buerstedde JM, Sommer SS: Functionally important regions of the factor IX gene have a low rate of polymorphism and a high rate of mutation in the dinucleotide CpG. Am J Hum Genet. 1989 Sep;45(3):448-57.
  30. 2775660 Liddell MB, Peake IR, Taylor SA, Lillicrap DP, Giddings JC, Bloom AL: Factor IX Cardiff: a variant factor IX protein that shows abnormal activation is caused by an arginine to cysteine substitution at position 145. Br J Haematol. 1989 Aug;72(4):556-60.
  31. 2994716 Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry. 1985 Jul 2;24(14):3736-50.
  32. 3009023 Bentley AK, Rees DJ, Rizza C, Brownlee GG: Defective propeptide processing of blood clotting factor IX caused by mutation of arginine to glutamine at position -4. Cell. 1986 May 9;45(3):343-8.
  33. 3243764 Sugimoto M, Miyata T, Kawabata S, Yoshioka A, Fukui H, Takahashi H, Iwanaga S: Blood clotting factor IX Niigata: substitution of alanine-390 by valine in the catalytic domain. J Biochem (Tokyo). 1988 Dec;104(6):878-80.
  34. 3340835 Stoflet ES, Koeberl DD, Sarkar G, Sommer SS: Genomic amplification with transcript sequencing. Science. 1988 Jan 29;239(4839):491-4.
  35. 3401602 Ware J, Davis L, Frazier D, Bajaj SP, Stafford DW: Genetic defect responsible for the dysfunctional protein: factor IXLong Beach. Blood. 1988 Aug;72(2):820-2.
  36. 3790720 Davis LM, McGraw RA, Ware JL, Roberts HR, Stafford DW: Factor IXAlabama: a point mutation in a clotting protein results in hemophilia B. Blood. 1987 Jan;69(1):140-3.
  37. 3857619 McGraw RA, Davis LM, Noyes CM, Lundblad RL, Roberts HR, Graham JB, Stafford DW: Evidence for a prevalent dimorphism in the activation peptide of human coagulation factor IX. Proc Natl Acad Sci U S A. 1985 May;82(9):2847-51.
  38. 6089357 Jagadeeswaran P, Lavelle DE, Kaul R, Mohandas T, Warren ST: Isolation and characterization of human factor IX cDNA: identification of Taq I polymorphism and regional assignment. Somat Cell Mol Genet. 1984 Sep;10(5):465-73.
  39. 6329734 Anson DS, Choo KH, Rees DJ, Giannelli F, Gould K, Huddleston JA, Brownlee GG: The gene structure of human anti-haemophilic factor IX. EMBO J. 1984 May;3(5):1053-60.
  40. 6425296 Morita T, Isaacs BS, Esmon CT, Johnson AE: Derivatives of blood coagulation factor IX contain a high affinity Ca2+-binding site that lacks gamma-carboxyglutamic acid. J Biol Chem. 1984 May 10;259(9):5698-704.
  41. 659613 Di Scipio RG, Kurachi K, Davie EW: Activation of human factor IX (Christmas factor). J Clin Invest. 1978 Jun;61(6):1528-38.
  42. 6603618 Noyes CM, Griffith MJ, Roberts HR, Lundblad RL: Identification of the molecular defect in factor IX Chapel Hill: substitution of histidine for arginine at position 145. Proc Natl Acad Sci U S A. 1983 Jul;80(14):4200-2.
  43. 6687940 Jaye M, de la Salle H, Schamber F, Balland A, Kohli V, Findeli A, Tolstoshev P, Lecocq JP: Isolation of a human anti-haemophilic factor IX cDNA clone using a unique 52-base synthetic oligonucleotide probe deduced from the amino acid sequence of bovine factor IX. Nucleic Acids Res. 1983 Apr 25;11(8):2325-35.
  44. 6688526 McMullen BA, Fujikawa K, Kisiel W: The occurrence of beta-hydroxyaspartic acid in the vitamin K-dependent blood coagulation zymogens. Biochem Biophys Res Commun. 1983 Aug 30;115(1):8-14.
  45. 7547952 Freedman SJ, Furie BC, Furie B, Baleja JD: Structure of the calcium ion-bound gamma-carboxyglutamic acid-rich domain of factor IX. Biochemistry. 1995 Sep 26;34(38):12126-37.
  46. 7606779 Rao Z, Handford P, Mayhew M, Knott V, Brownlee GG, Stuart D: The structure of a Ca(2+)-binding epidermal growth factor-like domain: its role in protein-protein interactions. Cell. 1995 Jul 14;82(1):131-41.
  47. 7713897 Freedman SJ, Furie BC, Furie B, Baleja JD: Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy. J Biol Chem. 1995 Apr 7;270(14):7980-7.
  48. 7981722 Caglayan SH, Vielhaber E, Gursel T, Aktuglu G, Sommer SS: Identification of mutations in four hemophilia B patients of Turkish origin, including a novel deletion of base 6411. Hum Mutat. 1994;4(2):163-5.
  49. 8076946 Aguilar-Martinez P, Romey MC, Schved JF, Gris JC, Demaille J, Claustres M: Factor IX gene mutations causing haemophilia B: comparison of SSC screening versus systematic DNA sequencing and diagnostic applications. Hum Genet. 1994 Sep;94(3):287-90.
  50. 8199596 Aguilar-Martinez P, Romey MC, Gris JC, Schved JF, Demaille J, Claustres M: A novel mutation (Val-373 to Glu) in the catalytic domain of factor IX, resulting in moderately/severe hemophilia B in a southern French patient. Hum Mutat. 1994;3(2):156-8.
  51. 8236150 de la Salle C, Charmantier JL, Baas MJ, Schwartz A, Wiesel ML, Grunebaum L, Cazenave JP: A deletion located in the 3' non translated part of the factor IX gene responsible for mild haemophilia B. Thromb Haemost. 1993 Aug 2;70(2):370-1.
  52. 8257988 David D, Rosa HA, Pemberton S, Diniz MJ, Campos M, Lavinha J: Single-strand conformation polymorphism (SSCP) analysis of the molecular pathology of hemophilia B. Hum Mutat. 1993;2(5):355-61.
  53. 8295821 de la Salle C, Charmantier JL, Ravanat C, Ohlmann P, Hartmann ML, Schuhler S, Bischoff R, Ebel C, Roecklin D, Balland A, et al.: The Arg-4 mutant factor IX Strasbourg 2 shows a delayed activation by factor XIa. Nouv Rev Fr Hematol. 1993;35(5):473-80.
  54. 8392713 Giannelli F, Green PM, High KA, Sommer S, Poon MC, Ludwig M, Schwaab R, Reitsma PH, Goossens M, Yoshioka A, et al.: Haemophilia B: database of point mutations and short additions and deletions--fourth edition, 1993. Nucleic Acids Res. 1993 Jul 1;21(13):3075-87.
  55. 8663165 Freedman SJ, Blostein MD, Baleja JD, Jacobs M, Furie BC, Furie B: Identification of the phospholipid binding site in the vitamin K-dependent blood coagulation protein factor IX. J Biol Chem. 1996 Jul 5;271(27):16227-36.
  56. 8680410 Wulff K, Schroder W, Wehnert M, Herrmann FH: Twenty-five novel mutations of the factor IX gene in haemophilia B. Hum Mutat. 1995;6(4):346-8.
  57. 8833911 Chu K, Wu SM, Stanley T, Stafford DW, High KA: A mutation in the propeptide of Factor IX leads to warfarin sensitivity by a novel mechanism. J Clin Invest. 1996 Oct 1;98(7):1619-25.
  58. 9047312 Li L, Darden TA, Freedman SJ, Furie BC, Furie B, Baleja JD, Smith H, Hiskey RG, Pedersen LG: Refinement of the NMR solution structure of the gamma-carboxyglutamic acid domain of coagulation factor IX using molecular dynamics simulation with initial Ca2+ positions determined by a genetic algorithm. Biochemistry. 1997 Feb 25;36(8):2132-8.
  59. 9222764 Caglayan SH, Gokmen Y, Aktuglu G, Gurgey A, Sommer SS: Mutations associated with hemophilia B in Turkish patients. Hum Mutat. 1997;10(1):76-9.
  60. 9452115 David D, Moreira I, Morais S, de Deus G: Five novel factor IX mutations in unrelated hemophilia B patients. Hum Mutat. 1998;Suppl 1:S301-3.
  61. 9590153 Chan V, Chan VW, Yip B, Chim CS, Chan TK: Hemophilia B in a female carrier due to skewed inactivation of the normal X-chromosome. Am J Hematol. 1998 May;58(1):72-6.
  62. 9600455 Heit JA, Thorland EC, Ketterling RP, Lind TJ, Daniels TM, Zapata RE, Ordonez SM, Kasper CK, Sommer SS: Germline mutations in Peruvian patients with hemophilia B: pattern of mutation in AmerIndians is similar to the putative endogenous germline pattern. Hum Mutat. 1998;11(5):372-6.
Target 3 Drug References
  1. Hule V: [Factor IX inhibitor (antihemophilic factor B, PTC) in a woman] Vnitr Lek. 1975 Mar;21(3):274-7. [PubMed Link Image]
  2. LUNDBLAD RL, DAVIE EW: THE ACTIVATION OF ANTIHEMOPHILIC FACTOR (FACTOR 8) BY ACTIVATED CHRISTMAS FACTOR (ACTIVATED FACTOR9 9). Biochemistry. 1964 Nov;3:1720-5. [PubMed Link Image]
  3. Yoshitake S, Schach BG, Foster DC, Davie EW, Kurachi K: Nucleotide sequence of the gene for human factor IX (antihemophilic factor B). Biochemistry. 1985 Jul 2;24(14):3736-50. [PubMed Link Image]
  4. Prince AM, Horowitz B, Brotman B, Huima T, Richardson L, van den Ende MC: Inactivation of hepatitis B and Hutchinson strain non-A, non-B hepatitis viruses by exposure to Tween 80 and ether. Vox Sang. 1984;46(1):36-43. [PubMed Link Image]
  5. Hoofnagle JH, Gerety RJ, Thiel J, Barker LF: The prevalence of hepatitis B surface antigen in commercially prepared plasma products. J Lab Clin Med. 1976 Jul;88(1):102-13. [PubMed Link Image]
Drug Target 4 [top]
Target 4 ID 422
Target 4 Name Vitamin K-dependent protein C
Target 4 Synonyms
  1. Anticoagulant protein C
  2. Autoprothrombin IIA
  3. Blood coagulation factor XIV
  4. EC 3.4.21.69
  5. Vitamin K-dependent protein C precursor
Target 4 Gene Name PROC
Target 4 Protein Sequence >Vitamin K-dependent protein C precursor
MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECI
EEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSC
DCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVK
FPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGA
VLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDI
ALLHLAQPATLSQTIVPICLPDSGLAERELNQAGQETLVTGWGYHSSREKEAKRNRTFVL
NFIKIPVVPHNECSEVMSNMVSENMLCAGILGDRQDACEGDSGGPMVASFHGTWFLVGLV
SWGEGCGLLHNYGVYTKVSRYLDWIHGHIRDKEAPQKSWAP
Target 4 Number of Residues 468
Target 4 Molecular Weight 52072
Target 4 Theoretical pI 6.23
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
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
proteolysis
physiological process
organismal physiological process
regulation of body fluids
hemostasis
blood coagulation
Component
extracellular region
Target 4 General Function Involved in calcium ion binding
Target 4 Specific Function Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids
Target 4 Pathways Not Available
Target 4 Reactions
  • Degradation of blood coagulation factors Va and VIIIa
Target 4 Pfam Domain Function
Target 4 Signals
  • 1-32
Target 4 Transmembrane Regions
  • None
Target 4 Essentiality Non-Essential
Target 4 GenBank ID Protein 190334 Link Image
Target 4 UniProtKB/Swiss-Prot ID P04070 Link Image
Target 4 UniProtKB/Swiss-Prot Entry Name PROC_HUMAN Link Image
Target 4 PDB ID 1AUT Link Image
Target 4 PDB File Show
Target 4 3D Structure
Target 4 Cellular Location
  • Cytoplasmic
Target 4 Gene Sequence >1386 bp
ATGTGGCAGCTCACAAGCCTCCTGCTGTTCGTGGCCACCTGGGGAATTTCCGGCACACCA
GCTCCTCTTGACTCAGTGTTCTCCAGCAGCGAGCGTGCCCACCAGGTGCTGCGGATCCGC
AAACGTGCCAACTCCTTCCTGGAGGAGCTCCGTCACAGCAGCCTGGAGCGGGAGTGCATA
GAGGAGATCTGTGACTTCGAGGAGGCCAAGGAAATTTTCCAAAATGTGGATGACACACTG
GCCTTCTGGTCCAAGCACGTCGACGGTGACCAGTGCTTGGTCTTGCCCTTGGAGCACCCG
TGCGCCAGCCTGTGCTGCGGGCACGGCACGTGCATCGACGGCATCGGCAGCTTCAGCTGC
GACTGCCGCAGCGGCTGGGAGGGCCGCTTCTGCCAGCGCGAGGTGAGCTTCCTCAATTGC
TCTCTGGACAACGGCGGCTGCACGCATTACTGCCTAGAGGAGGTGGGCTGGCGGCGCTGT
AGCTGTGCGCCTGGCTACAAGCTGGGGGACGACCTCCTGCAGTGTCACCCCGCAGTGAAG
TTCCCTTGTGGGAGGCCCTGGAAGCGGATGGAGAAGAAGCGCAGTCACCTGAAACGAGAC
ACAGAAGACCAAGAAGACCAAGTAGATCCGCGGCTCATTGATGGGAAGATGACCAGGCGG
GGAGACAGCCCCTGGCAGGTGGTCCTGCTGGACTCAAAGAAGAAGCTGGCCTGCGGGGCA
GTGCTCATCCACCCCTCCTGGGTGCTGACAGCGGCCCACTGCATGGATGAGTCCAAGAAG
CTCCTTGTCAGGCTTGGAGAGTATGACCTGCGGCGCTGGGAGAAGTGGGAGCTGGACCTG
GACATCAAGGAGGTCTTCGTCCACCCCAACTACAGCAAGAGCACCACCGACAATGACATC
GCACTGCTGCACCTGGCCCAGCCCGCCACCCTCTCGCAGACCATAGTGCCCATCTGCCTC
CCGGACAGCGGCCTTGCAGAGCGCGAGCTCAATCAGGCCGGCCAGGAGACCCTCGTGACG
GGCTGGGGCTACCACAGCAGCCGAGAGAAGGAGGCCAAGAGAAACCGCACCTTCGTCCTC
AACTTCATCAAGATTCCCGTGGTCCCGCACAATGAGTGCAGCGAGGTCATGAGCAACATG
GTGTCTGAGAACATGCTGTGTGCGGGCATCCTCGGGGACCGGCAGGATGCCTGCGAGGGC
GACAGTGGGGGGCCCATGGTCGCCTCCTTCCACGGCACCTGGTTCCTGGTGGGCCTGGTG
AGCTGGGGTGAGGGCTGTGGGCTCCTTCACAACTACGGCGTTTACACCAAAGTCAGCCGC
TACCTCGACTGGATCCATGGGCACATCAGAGACAAGGAAGCCCCCCAGAAGAGCTGGGCA
CCTTAG
Target 4 GenBank Gene ID
Target 4 GeneCard ID PROC Link Image
Target 4 GenAtlas ID PROC Link Image
Target 4 HGNC ID HGNC:9451 Link Image
Target 4 Chromosome Location 2
Target 4 Locus 2q13-q14
Target 4 SNPs SNPJam Report Link Image
Target 4 General References
  1. Gandrille S, Vidaud M, Aiach M, Alhenc-Gelas M, Fischer AM, Gouault-Heilman M, Toulon P, Fiessinger JN, Goossens M: Two novel mutations responsible for hereditary type I protein C deficiency: characterization by denaturing gradient gel electrophoresis. Hum Mutat. 1992;1(6):491-500. [PubMed Link Image]
  2. Bovill EG, Tomczak JA, Grant B, Bhushan F, Pillemer E, Rainville IR, Long GL: Protein CVermont: symptomatic type II protein C deficiency associated with two GLA domain mutations. Blood. 1992 Mar 15;79(6):1456-65. [PubMed Link Image]
  3. Grundy CB, Chisholm M, Kakkar VV, Cooper DN: A novel homozygous missense mutation in the protein C (PROC) gene causing recurrent venous thrombosis. Hum Genet. 1992 Aug;89(6):683-4. [PubMed Link Image]
  4. Grundy CB, Schulman S, Tengborn L, Kakkar VV, Cooper DN: Two different missense mutations at Arg 178 of the protein C (PROC) gene causing recurrent venous thrombosis. Hum Genet. 1992 Aug;89(6):685-6. [PubMed Link Image]
  5. Harris RJ, Ling VT, Spellman MW: O-linked fucose is present in the first epidermal growth factor domain of factor XII but not protein C. J Biol Chem. 1992 Mar 15;267(8):5102-7. [PubMed Link Image]
  6. Yamamoto K, Matsushita T, Sugiura I, Takamatsu J, Iwasaki E, Wada H, Deguchi K, Shirakawa S, Saito H: Homozygous protein C deficiency: identification of a novel missense mutation that causes impaired secretion of the mutant protein C. J Lab Clin Med. 1992 Jun;119(6):682-9. [PubMed Link Image]
  7. Sugahara Y, Miura O, Yuen P, Aoki N: Protein C deficiency Hong Kong 1 and 2: hereditary protein C deficiency caused by two mutant alleles, a 5-nucleotide deletion and a missense mutation. Blood. 1992 Jul 1;80(1):126-33. [PubMed Link Image]
  8. Miletich JP, Broze GJ Jr: Beta protein C is not glycosylated at asparagine 329. The rate of translation may influence the frequency of usage at asparagine-X-cysteine sites. J Biol Chem. 1990 Jul 5;265(19):11397-404. [PubMed Link Image]
  9. Reitsma PH, Poort SR, Allaart CF, Briet E, Bertina RM: The spectrum of genetic defects in a panel of 40 Dutch families with symptomatic protein C deficiency type I: heterogeneity and founder effects. Blood. 1991 Aug 15;78(4):890-4. [PubMed Link Image]
  10. Romeo G, Hassan HJ, Staempfli S, Roncuzzi L, Cianetti L, Leonardi A, Vicente V, Mannucci PM, Bertina R, Peschle C, et al.: Hereditary thrombophilia: identification of nonsense and missense mutations in the protein C gene. Proc Natl Acad Sci U S A. 1987 May;84(9):2829-32. [PubMed Link Image]
  11. 2602169 Grundy C, Chitolie A, Talbot S, Bevan D, Kakkar V, Cooper DN: Protein C London 1: recurrent mutation at Arg 169 (CGG----TGG) in the protein C gene causing thrombosis. Nucleic Acids Res. 1989 Dec 25;17(24):10513.
  12. 2991859 Beckmann RJ, Schmidt RJ, Santerre RF, Plutzky J, Crabtree GR, Long GL: The structure and evolution of a 461 amino acid human protein C precursor and its messenger RNA, based upon the DNA sequence of cloned human liver cDNAs. Nucleic Acids Res. 1985 Jul 25;13(14):5233-47.
  13. 2991887 Foster DC, Yoshitake S, Davie EW: The nucleotide sequence of the gene for human protein C. Proc Natl Acad Sci U S A. 1985 Jul;82(14):4673-7.
  14. 3511471 Plutzky J, Hoskins JA, Long GL, Crabtree GR: Evolution and organization of the human protein C gene. Proc Natl Acad Sci U S A. 1986 Feb;83(3):546-50.
  15. 6589623 Foster D, Davie EW: Characterization of a cDNA coding for human protein C. Proc Natl Acad Sci U S A. 1984 Aug;81(15):4766-70.
  16. 7605880 Millar DS, Bevan D, Chitolie A, Reynaud J, Chisholm M, Kakkar VV, Cooper DN: Three novel mutations in the protein C (PROC) gene causing venous thrombosis. Blood Coagul Fibrinolysis. 1995 Apr;6(2):138-40.
  17. 7792728 Lind B, Schwartz M, Thorsen S: Six different point mutations in seven Danish families with symptomatic protein C deficiency. Thromb Haemost. 1995 Feb;73(2):186-93.
  18. 7841323 Millar DS, Allgrove J, Rodeck C, Kakkar VV, Cooper DN: A homozygous deletion/insertion mutation in the protein C (PROC) gene causing neonatal Purpura fulminans: prenatal diagnosis in an at-risk pregnancy. Blood Coagul Fibrinolysis. 1994 Aug;5(4):647-9.
  19. 7841324 Witt I, Beck S, Seydewitz HH, Tasangil C, Schenck W: A novel homozygous missense mutation (Val 325-->Ala) in the protein C gene causing neonatal purpura fulminans. Blood Coagul Fibrinolysis. 1994 Aug;5(4):651-3.
  20. 7865674 Zheng YZ, Sakata T, Matsusue T, Umeyama H, Kato H, Miyata T: Six missense mutations associated with type I and type II protein C deficiency and implications obtained from molecular modelling. Blood Coagul Fibrinolysis. 1994 Oct;5(5):687-96.
  21. 7878626 Long GL, Tomczak JA, Rainville IR, Dreyfus M, Schramm W, Schwarz HP: Homozygous type I protein C deficiency in two unrelated families exhibiting thrombophilia related to Ala136-->Pro or Arg286-->His mutations. Thromb Haemost. 1994 Oct;72(4):526-33.
  22. 7919373 Gandrille S, Jude B, Alhenc-Gelas M, Emmerich J, Aiach M: First de novo mutations in the protein C gene of two patients with type I deficiency: a missense mutation and a splice site deletion. Blood. 1994 Oct 15;84(8):2566-70.
  23. 7974343 Gaussem P, Gandrille S, Duchemin J, Emmerich J, Alhenc-Gelas M, Aillaud MF, Aiach M: Influence of six mutations of the protein C gene on the Gla domain conformation and calcium affinity. Thromb Haemost. 1994 Jun;71(6):748-54.
  24. 8003977 Fisher CL, Greengard JS, Griffin JH: Models of the serine protease domain of the human antithrombotic plasma factor activated protein C and its zymogen. Protein Sci. 1994 Apr;3(4):588-99.
  25. 8292730 Tsay W, Greengard JS, Montgomery RR, McPherson RA, Fucci JC, Koerper MA, Coughlin J, Griffin JH: Genetic mutations in ten unrelated American patients with symptomatic type 1 protein C deficiency. Blood Coagul Fibrinolysis. 1993 Oct;4(5):791-6.
  26. 8324221 Gandrille S, Alhenc-Gelas M, Gaussem P, Aillaud MF, Dupuy E, Juhan-Vague I, Aiach M: Five novel mutations located in exons III and IX of the protein C gene in patients presenting with defective protein C anticoagulant activity. Blood. 1993 Jul 1;82(1):159-68.
  27. 8398832 Marchetti G, Patracchini P, Gemmati D, Castaman G, Rodeghiero F, Wacey A, Cooper DN, Tuddenham EG, Bernardi F: Symptomatic type II protein C deficiency caused by a missense mutation (Gly 381-->Ser) in the substrate-binding pocket. Br J Haematol. 1993 Jun;84(2):285-9.
  28. 8446940 Reitsma PH, Poort SR, Bernardi F, Gandrille S, Long GL, Sala N, Cooper DN: Protein C deficiency: a database of mutations. For the Protein C & S Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb Haemost. 1993 Jan 11;69(1):77-84.
  29. 8477066 Mimuro J, Muramatsu S, Kaneko M, Yoshitake S, Iijima K, Nakamura K, Sakata Y, Matsuda M: An abnormal protein C (protein C Yonago) with an amino acid substitution of Gly for Arg-15 caused by a single base mutation of C to G in codon 57 (CGG-->GGG). Deteriorated calcium-dependent conformation of the gamma-carboxyglutamic acid domain relevant to a thrombotic tendency. Int J Hematol. 1993 Jan;57(1):9-14.
  30. 8499565 Poort SR, Pabinger-Fasching I, Mannhalter C, Reitsma PH, Bertina RM: Twelve novel and two recurrent mutations in 14 Austrian families with hereditary protein C deficiency. Blood Coagul Fibrinolysis. 1993 Apr;4(2):273-80.
  31. 8499568 Millar DS, Grundy CB, Bignell P, Moffat EH, Martin R, Kakkar VV, Cooper DN: A Gla domain mutation (Arg 15-->Trp) in the protein C (PROC) gene causing type 2 protein C deficiency and recurrent venous thrombosis. Blood Coagul Fibrinolysis. 1993 Apr;4(2):345-7.
  32. 8829639 Ireland HA, Boisclair MD, Taylor J, Thompson E, Thein SL, Girolami A, De Caterina M, Scopacasa F, De Stefano V, Leone G, Finazzi G, Cohen H, Lane DA: Two novel (R(-11)C; T394D) and two repeat missense mutations in the protein C gene associated with venous thrombosis in six kindreds. Hum Mutat. 1996;7(2):176-9.
  33. 9003757 Mather T, Oganessyan V, Hof P, Huber R, Foundling S, Esmon C, Bode W: The 2.8 A crystal structure of Gla-domainless activated protein C. EMBO J. 1996 Dec 16;15(24):6822-31.
  34. 9798967 Couture P, Demers C, Morissette J, Delage R, Jomphe M, Couture L, Simard J: Type I protein C deficiency in French Canadians: evidence of a founder effect and association of specific protein C gene mutations with plasma protein C levels. Thromb Haemost. 1998 Oct;80(4):551-6.
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 1245
Target 5 Name Vitamin K-dependent protein S
Target 5 Synonyms
  1. Vitamin K-dependent protein S precursor
Target 5 Gene Name PROS1
Target 5 Protein Sequence >Vitamin K-dependent protein S precursor
MRVLGGRCGALLACLLLVLPVSEANFLSKQQASQVLVRKRRANSLLEETKQGNLERECIE
ELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQ
CSPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPG
SYHCSCKNGFVMLSNKKDCKDVDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKS
CEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKSCEVVSVCLPLNLDTKYELL
YLAEQFAGVVLYLKFRLPEISRFSAEFDFRTYDSEGVILYAESIDHSAWLLIALRGGKIE
VQLKNEHTSKITTGGDVINNGLWNMVSVEELEHSISIKIAKEAVMDINKPGPLFKPENGL
LETKVYFAGFPRKVESELIKPINPRLDGCIRSWNLMKQGASGIKEIIQEKQNKHCLVTVE
KGSYYPGSGIAQFHIDYNNVSSAEGWHVNVTLNIRPSTGTGVMLALVSGNNTVPFAVSLV
DSTSEKSQDILLSVENTVIYRIQALSLCSDQQSHLEFRVNRNNLELSTPLKIETISHEDL
QRQLAVLDKAMKAKVATYLGGLPDVPFSATPVNAFYNGCMEVNINGVQLDLDEAISKHND
IRAHSCPSVWKKTKNS
Target 5 Number of Residues 687
Target 5 Molecular Weight 75123
Target 5 Theoretical pI 5.37
Target 5 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
extracellular region
Target 5 General Function Involved in calcium ion binding
Target 5 Specific Function Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis
Target 5 Pathways Not Available
Target 5 Reactions Not Available
Target 5 Pfam Domain Function
Target 5 Signals
  • 1-24
Target 5 Transmembrane Regions
  • None
Target 5 Essentiality Non-Essential
Target 5 GenBank ID Protein 190289 Link Image
Target 5 UniProtKB/Swiss-Prot ID P07225 Link Image
Target 5 UniProtKB/Swiss-Prot Entry Name PROS_HUMAN Link Image
Target 5 PDB ID Not Available
Target 5 Cellular Location
  • Secreted protein
Target 5 Gene Sequence >2031 bp
ATGAGGGTCCTGGGTGGGCGCTGCGGGGCGCCGCTGGCGTGTCTCCTCCTAGTGCTTCCC
GTCTCAGAGGCAAACCTTCTGTCAAAGCAACAGGCTTCACAAGTCCTGGTTAGGAAGCGT
CGTGCAAATTCTTTACTTGAAGAAACCAAACAGGGTAATCTTGAAAGAGAATGCATCGAA
GAACTGTGCAATAAAGAAGAAGCCAGGGAGGTCTTTGAAAATGACCCGGAAACGGATTAT
TTTTATCCAAAATACTTAGTTTGTCTTCGCTCTTTTCAAACTGGGTTATTCACTGCTGCA
CGTCAGTCAACTAATGCTTATCCTGACCTAAGAAGCTGTGTCAATGCCATTCCAGACCAG
TGTAGTCCTCTGCCATGCAATGAAGATGGATATATGAGCTGCAAAGATGGAAAAGCTTCT
TTTACTTGCACTTGTAAACCAGGTTGGCAAGGAGAAAAGTGTGAATTTGACATAAATGAA
TGCAAAGATCCCTCAAATATAAATGGAGGTTGCAGTCAAATTTGTGATAATACACCTGGA
AGTTACCACTGTTCCTGTAAAAATGGTTTTGTTATGCTTTCAAATAAGAAAGATTGTAAA
GATGTGGATGAATGCTCTTTGAAGCCAAGCATTTGTGGCACAGCTGTGTGCAAGAACATC
CCAGGAGATTTTGAATGTGAATGCCCCGAAGGCTACAGATATAATCTCAAATCAAAGTCT
TGTGAAGATATAGATGAATGCTCTGAGAACATGTGTGCTCAGCTTTGTGTCAATTACCCT
GGAGGTTACACTTGCTATTGTGATGGGAAGAAAGGATTCAAACTTGCCCAAGATCAGAAG
AGTTGTGAGGTTGTTTCAGTGTGCCTTCCCTTGAACCTTGACACAAAGTATGAATTACTT
TACTTGGCGGAGCAGTTTGCAGGGGTTGTTTTATATTTAAAATTTCGTTTGCCAGAAATC
AGCAGATTTTCAGCAGAATTTGATTTCCGGACATATGATTCAGAAGGCGTGATACTGTAC
GCAGAATCTATCGATCACTCAGCGTGGCTCCTGATTGCACTTCGTGGTGGAAAGATTGAA
GTTCAGCTTAAGAATGAACATACATCCAAAATCACAACTGGAGGTGATGTTATTAATAAT
GGTCTATGGAATATGGTGTCTGTGGAAGAATTAGAACATAGTATTAGCATTAAAATAGCT
AAAGAAGCTGTGATGGATATAAATAAACCTGGACCCCTTTTTAAGCCGGAAAATGGATTG
CTGGAAACCAAAGTATACTTTGCAGGATTCCCTCGGAAAGTGGAAAGTGAACTCATTAAA
CCGATTAACCCTCGTCTAGATGGATGTATACGAAGCTGGAATTTGATGAAGCAAGGAGCT
TCTGGAATAAAGGAAATTATTCAAGAAAAACAAAATAAGCATTGCCTGGTTACTGTGGAG
AAGGGCTCCTACTATCCTGGTTCTGGAATTGCTCAATTTCACATAGATTATAATAATGTA
TCCAGTGCTGAGGGTTGGCATGTAAATGTGACCTTGAATATTCGTCCATCCACGGGCACT
GGTGTTATGCTTGCCTTGGTTTCTGGTAACAACACAGTGCCCTTTGCTGTGTCCTTGGTG
GACTCCACCTCTGAAAAATCACAGGATATTCTGTTATCTGTTGAAAATACTGTAATATAT
CGGATACAGGCCCTAAGTCTATGTTCCGATCAACAATCTCATCTGGAATTTAGAGTCAAC
AGAAACAATCTGGAGTTGTCGACACCACTTAAAATAGAAACCATCTCCCATGAAGACCTT
CAAAGACAACTTGCCGTCTTGGACAAAGCAATGAAAGCAAAAGTGGCCACATACCTGGGT
GGCCTTCCAGATGTTCCATTCAGTGCCACACCAGTGAATGCCTTTTATAATGGCTGCATG
GAAGTGAATATTAATGGTGTACAGTTGGATCTGGATGAAGCCATTTCTAAACATAATGAT
ATTAGAGCTCACTCATGTCCATCAGTTTGGAAAAAGACAAAGAATTCTTAA
Target 5 GenBank Gene ID
Target 5 GeneCard ID PROS1 Link Image
Target 5 GenAtlas ID PROS1 Link Image
Target 5 HGNC ID HGNC:9456 Link Image
Target 5 Chromosome Location 3
Target 5 Locus 3q11.2
Target 5 SNPs SNPJam Report Link Image
Target 5 General References
  1. Espinosa-Parrilla Y, Morell M, Souto JC, Tirado I, Fontcuberta J, Estivill X, Sala N: Protein S gene analysis reveals the presence of a cosegregating mutation in most pedigrees with type I but not type III PS deficiency. Hum Mutat. 1999;14(1):30-9. [PubMed Link Image]
  2. Bertina RM, Ploos van Amstel HK, van Wijngaarden A, Coenen J, Leemhuis MP, Deutz-Terlouw PP, van der Linden IK, Reitsma PH: Heerlen polymorphism of protein S, an immunologic polymorphism due to dimorphism of residue 460. Blood. 1990 Aug 1;76(3):538-48. [PubMed Link Image]
  3. Schmidel DK, Tatro AV, Phelps LG, Tomczak JA, Long GL: Organization of the human protein S genes. Biochemistry. 1990 Aug 28;29(34):7845-52. [PubMed Link Image]
  4. Ploos van Amstel HK, Reitsma PH, van der Logt CP, Bertina RM: Intron-exon organization of the active human protein S gene PS alpha and its pseudogene PS beta: duplication and silencing during primate evolution. Biochemistry. 1990 Aug 28;29(34):7853-61. [PubMed Link Image]
  5. Ploos van Amstel HK, van der Zanden AL, Reitsma PH, Bertina RM: Human protein S cDNA encodes Phe-16 and Tyr 222 in consensus sequences for the post-translational processing. FEBS Lett. 1987 Sep 28;222(1):186-90. [PubMed Link Image]
  6. Lundwall A, Dackowski W, Cohen E, Shaffer M, Mahr A, Dahlback B, Stenflo J, Wydro R: Isolation and sequence of the cDNA for human protein S, a regulator of blood coagulation. Proc Natl Acad Sci U S A. 1986 Sep;83(18):6716-20. [PubMed Link Image]
  7. Hoskins J, Norman DK, Beckmann RJ, Long GL: Cloning and characterization of human liver cDNA encoding a protein S precursor. Proc Natl Acad Sci U S A. 1987 Jan;84(2):349-53. [PubMed Link Image]
  8. Hayashi T, Nishioka J, Shigekiyo T, Saito S, Suzuki K: Protein S Tokushima: abnormal molecule with a substitution of Glu for Lys-155 in the second epidermal growth factor-like domain of protein S. Blood. 1994 Feb 1;83(3):683-90. [PubMed Link Image]
Target 5 Drug References
  1. Siegert G, Kostka H, Gehrisch S, Schwarz T, Schellong S, Jaross W: Method-dependent influence of certain polymorphisms in the factor V B-domain on the response to activated protein C. Blood Coagul Fibrinolysis. 2000 Sep;11(6):519-27. [PubMed Link Image]
Drug Target 6 [top]
Target 6 ID 1516
Target 6 Name Calnexin
Target 6 Synonyms
  1. Calnexin precursor
  2. IP90
  3. Major histocompatibility complex class I antigen- binding protein p88
  4. p90
Target 6 Gene Name CANX
Target 6 Protein Sequence >Calnexin precursor
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTY
KAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGL
VLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFH
DKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTL
ILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVK
PDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRC
ESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFS
AIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEER
PWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDE
EEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
Target 6 Number of Residues 601
Target 6 Molecular Weight 67569
Target 6 Theoretical pI 4.21
Target 6 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 6 General Function Involved in calcium ion binding
Target 6 Specific Function Calcium-binding protein that interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins
Target 6 Pathways Not Available
Target 6 Reactions Not Available
Target 6 Pfam Domain Function
Target 6 Signals
  • 1-20
Target 6 Transmembrane Regions
  • 482-502
Target 6 Essentiality Non-Essential
Target 6 GenBank ID Protein 186523 Link Image
Target 6 UniProtKB/Swiss-Prot ID P27824 Link Image
Target 6 UniProtKB/Swiss-Prot Entry Name CALX_HUMAN Link Image
Target 6 PDB ID 1JHN Link Image
Target 6 PDB File Show
Target 6 3D Structure
Target 6 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum membrane
  • single-pass type I membrane protein. Melanoso
Target 6 Gene Sequence >1779 bp
ATGGAAGGGAAGTGGTTGCTGTGTATGTTACTGGTGCTTGGAACTGCTATTGTTGAGGCT
CATGATGGACATGATGATGATGTGATTGATATTGAGGATGACCTTGACGATGTCATTGAA
GAGGTAGAAGACTCAAAACCAGATACCACTGCTCCTCCTTCATCTCCCAAGGTTACTTAC
AAAGCTCCAGTTCCAACAGGGGAAGTATATTTTGCTGATTCTTTTGACAGAGGAACTCTG
TCAGGGTGGATTTTATCCAAAGCCAAGAAAGACGATACCGATGATGAAATTGCCAAATAT
GATGGAAAGTGGGAGGTAGAGGAAATGAAGGAGTCAAAGCTTCCAGGTGATAAAGGACTT
GTGTTGATGTCTCGGGCCAAGCATCATGCGATCTCTGCTAAACTGAACAAGCCCTTCCTG
TTTGACACCAAGCCTCTCATTGTTCAGTATGAGGTTAATTTCCAAAATGGAATAGAATGT
GGTGGTGCCTATGTGAAACTGCTTTCTAAAACACCAGAACTCAACCTGGATCAGTTCCAT
GACAAGACCCCTTATACGATTATGTTTGGTCCAGATAAATGTGGAGAGGACTATAAACTG
CACTTCATCTTCCGACACAAAAACCCCAAAACGGGTATCTATGAAGAAAAACATGCTAAG
AGGCCAGATGCAGATCTGAAGACCTATTTTACTGATAAGAAAACACATCTTTACACACTA
ATCTTGAATCCAGATAATAGTTTTGAAATACTGGTTGACCAATCTGTGGTGAATAGTGGA
AATCTGCTCAATGACATGACTCCTCCTGTAAATCCTTCACGTGAAATTGAGGACCCAGAA
GACCGGAAGCCCGAGGATTGGGATGAAAGACCAAAAATCCCAGATCCAGAAGCTGTCAAG
CCAGATGACTGGGATGAAGATGCCCCTGCTAAGATTCCAGATGAAGAGGCCACAAAACCC
GAAGGCTGGTTAGATGATGAGCCTGAGTACGTACCTGATCCAGACGCAGAGAAACCTGAG
GATTGGGATGAAGACATGGATGGAGAATGGGAGGCTCCTCAGATTGCCAACCCTAGATGT
GAGTCAGCTCCTGGATGTGGTGTCTGGCAGCGACCTGTGATTGACAACCCCAATTATAAA
GGCAAATGGAAGCCTCCTATGATTGACAATCCCAGTTACCAGGGAATCTGGAAACCCAGG
AAAATACCAAATCCAGATTTCTTTGAAGATCTGGAACCTTTCAGAATGACTCCTTTTAGT
GCTATTGGTTTGGAGCTGTGGTCCATGACCTCTGACATTTTTTTTGACAACTTTATCATT
TGTGCTGATCGAAGAATAGTTGATGATTGGGCCAATGATGGATGGGGCCTGAAGAAAGCT
GCTGATGGGGCTGCTGAGCCAGGCGTTGTGGGGCAGATGATCGAGGCAGCTGAAGAGCGC
CCGTGGCTGTGGGTAGTCTATATTCTAACTGTAGCCCTTCCTGTGTTCCTGGTTATCCTC
TTCTGCTGTTCTGGAAAGAAACAGACCAGTGGTATGGAGTATAAGAAAACTGATGCACCT
CAACCGGATGTGAAGGAAGAGGAAGAAGAGAAGGAAGAGGAAAAGGACAAGGGAGATGAG
GAGGAGGAAGGAGAAGAGAAACTTGAAGAGAAACAGAAAAGTGATGCTGAAGAAGATGGT
GGCACTGTCAGTCAAGAGGAGGAAGACAGAAAACCTAAAGCAGAGGAGGATGAAATTTTG
AACAGATCACCAAGAAACAGAAAGCCACGAAGAGAGTGA
Target 6 GenBank Gene ID
Target 6 GeneCard ID CANX Link Image
Target 6 GenAtlas ID CANX Link Image
Target 6 HGNC ID HGNC:1473 Link Image
Target 6 Chromosome Location 5
Target 6 Locus 5q35
Target 6 SNPs SNPJam Report Link Image
Target 6 General References
  1. Rasmussen HH, van Damme J, Puype M, Gesser B, Celis JE, Vandekerckhove J: Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes. Electrophoresis. 1992 Dec;13(12):960-9. [PubMed Link Image]
  2. Galvin K, Krishna S, Ponchel F, Frohlich M, Cummings DE, Carlson R, Wands JR, Isselbacher KJ, Pillai S, Ozturk M: The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene. Proc Natl Acad Sci U S A. 1992 Sep 15;89(18):8452-6. [PubMed Link Image]
  3. Honore B, Rasmussen HH, Celis A, Leffers H, Madsen P, Celis JE: The molecular chaperones HSP28, GRP78, endoplasmin, and calnexin exhibit strikingly different levels in quiescent keratinocytes as compared to their proliferating normal and transformed counterparts: cDNA cloning and expression of calnexin. Electrophoresis. 1994 Mar-Apr;15(3-4):482-90. [PubMed Link Image]
  4. Tjoelker LW, Seyfried CE, Eddy RL Jr, Byers MG, Shows TB, Calderon J, Schreiber RB, Gray PW: Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5. Biochemistry. 1994 Mar 22;33(11):3229-36. [PubMed Link Image]
  5. David V, Hochstenbach F, Rajagopalan S, Brenner MB: Interaction with newly synthesized and retained proteins in the endoplasmic reticulum suggests a chaperone function for human integral membrane protein IP90 (calnexin). J Biol Chem. 1993 May 5;268(13):9585-92. [PubMed Link Image]
Target 6 Drug References
  1. Becker S, Simpson JC, Pepperkok R, Heinz S, Herder C, Grez M, Seifried E, Tonn T: Confocal microscopy analysis of native, full length and B-domain deleted coagulation factor VIII trafficking in mammalian cells. Thromb Haemost. 2004 Jul;92(1):23-35. [PubMed Link Image]
  2. 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]
  3. 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]
  4. Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2007 Sep 26;. [PubMed Link Image]
  5. Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [PubMed Link Image]
Drug Target 7 [top]
Target 7 ID 1635
Target 7 Name von Willebrand factor
Target 7 Synonyms
  1. vWF
  2. von Willebrand factor precursor
Target 7 Gene Name VWF
Target 7 Protein Sequence >von Willebrand factor precursor
MIPARFAGVLLALALILPGTLCAEGTRGRSSTARCSLFGSDFVNTFDGSMYSFAGYCSYL
LAGGCQKRSFSIIGDFQNGKRVSLSVYLGEFFDIHLFVNGTVTQGDQRVSMPYASKGLYL
ETEAGYYKLSGEAYGFVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGTL
TSDPYDFANSWALSSGEQWCERASPPSSSCNISSGEMQKGLWEQCQLLKSTSVFARCHPL
VDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGME
YRQCVSPCARTCQSLHINEMCQERCVDGCSCPEGQLLDEGLCVESTECPCVHSGKRYPPG
TSLSRDCNTCICRNSQWICSNEECPGECLVTGQSHFKSFDNRYFTFSGICQYLLARDCQD
HSFSIVIETVQCADDRDAVCTRSVTVRLPGLHNSLVKLKHGAGVAMDGQDIQLPLLKGDL
RIQHTVTASVRLSYGEDLQMDWDGRGRLLVKLSPVYAGKTCGLCGNYNGNQGDDFLTPSG
LAEPRVEDFGNAWKLHGDCQDLQKQHSDPCALNPRMTRFSEEACAVLTSPTFEACHRAVS
PLPYLRNCRYDVCSCSDGRECLCGALASYAAACAGRGVRVAWREPGRCELNCPKGQVYLQ
CGTPCNLTCRSLSYPDEECNEACLEGCFCPPGLYMDERGDCVPKAQCPCYYDGEIFQPED
IFSDHHTMCYCEDGFMHCTMSGVPGSLLPDAVLSSPLSHRSKRSLSCRPPMVKLVCPADN
LRAEGLECTKTCQNYDLECMSMGCVSGCLCPPGMVRHENRCVALERCPCFHQGKEYAPGE
TVKIGCNTCVCRDRKWNCTDHVCDATCSTIGMAHYLTFDGLKYLFPGECQYVLVQDYCGS
NPGTFRILVGNKGCSHPSVKCKKRVTILVEGGEIELFDGEVNVKRPMKDETHFEVVESGR
YIILLLGKALSVVWDRHLSISVVLKQTYQEKVCGLCGNFDGIQNNDLTSSNLQVEEDPVD
FGNSWKVSSQCADTRKVPLDSSPATCHNNIMKQTMVDSSCRILTSDVFQDCNKLVDPEPY
LDVCIYDTCSCESIGDCACFCDTIAAYAHVCAQHGKVVTWRTATLCPQSCEERNLRENGY
ECEWRYNSCAPACQVTCQHPEPLACPVQCVEGCHAHCPPGKILDELLQTCVDPEDCPVCE
VAGRRFASGKKVTLNPSDPEHCQICHCDVVNLTCEACQEPGGLVVPPTDAPVSPTTLYVE
DISEPPLHDFYCSRLLDLVFLLDGSSRLSEAEFEVLKAFVVDMMERLRISQKWVRVAVVE
YHDGSHAYIGLKDRKRPSELRRIASQVKYAGSQVASTSEVLKYTLFQIFSKIDRPEASRI
ALLLMASQEPQRMSRNFVRYVQGLKKKKVIVIPVGIGPHANLKQIRLIEKQAPENKAFVL
SSVDELEQQRDEIVSYLCDLAPEAPPPTLPPHMAQVTVGPGLLGVSTLGPKRNSMVLDVA
FVLEGSDKIGEADFNRSKEFMEEVIQRMDVGQDSIHVTVLQYSYMVTVEYPFSEAQSKGD
ILQRVREIRYQGGNRTNTGLALRYLSDHSFLVSQGDREQAPNLVYMVTGNPASDEIKRLP
GDIQVVPIGVGPNANVQELERIGWPNAPILIQDFETLPREAPDLVLQRCCSGEGLQIPTL
SPAPDCSQPLDVILLLDGSSSFPASYFDEMKSFAKAFISKANIGPRLTQVSVLQYGSITT
IDVPWNVVPEKAHLLSLVDVMQREGGPSQIGDALGFAVRYLTSEMHGARPGASKAVVILV
TDVSVDSVDAAADAARSNRVTVFPIGIGDRYDAAQLRILAGPAGDSNVVKLQRIEDLPTM
VTLGNSFLHKLCSGFVRICMDEDGNEKRPGDVWTLPDQCHTVTCQPDGQTLLKSHRVNCD
RGLRPSCPNSQSPVKVEETCGCRWTCPCVCTGSSTRHIVTFDGQNFKLTGSCSYVLFQNK
EQDLEVILHNGACSPGARQGCMKSIEVKHSALSVELHSDMEVTVNGRLVSVPYVGGNMEV
NVYGAIMHEVRFNHLGHIFTFTPQNNEFQLQLSPKTFASKTYGLCGICDENGANDFMLRD
GTVTTDWKTLVQEWTVQRPGQTCQPILEEQCLVPDSSHCQVLLLPLFAECHKVLAPATFY
AICQQDSCHQEQVCEVIASYAHLCRTNGVCVDWRTPDFCAMSCPPSLVYNHCEHGCPRHC
DGNVSSCGDHPSEGCFCPPDKVMLEGSCVPEEACTQCIGEDGVQHQFLEAWVPDHQPCQI
CTCLSGRKVNCTTQPCPTAKAPTCGLCEVARLRQNADQCCPEYECVCDPVSCDLPPVPHC
ERGLQPTLTNPGECRPNFTCACRKEECKRVSPPSCPPHRLPTLRKTQCCDEYECACNCVN
STVSCPLGYLASTATNDCGCTTTTCLPDKVCVHRSTIYPVGQFWEEGCDVCTCTDMEDAV
MGLRVAQCSQKPCEDSCRSGFTYVLHEGECCGRCLPSACEVVTGSPRGDSQSSWKSVGSQ
WASPENPCLINECVRVKEEVFIQQRNVSCPQLEVPVCPSGFQLSCKTSACCPSCRCERME
ACMLNGTVIGPGKTVMIDVCTTCRCMVQVGVISGFKLECRKTTCNPCPLGYKEENNTGEC
CGRCLPTACTIQLRGGQIMTLKRDETLQDGCDTHFCKVNERGEYFWEKRVTGCPPFDEHK
CLAEGGKIMKIPGTCCDTCEEPECNDITARLQYVKVGSCKSEVEVDIHYCQGKCASKAMY
SIDINDVQDQCSCCSPTRTEPMQVALHCTNGSVVYHEVLNAMECKCSPRKCSK
Target 7 Number of Residues 2859
Target 7 Molecular Weight 309301
Target 7 Theoretical pI 5.21
Target 7 GO Classification
Function
Not Available
Process
physiological process
organismal physiological process
regulation of body fluids
hemostasis
blood coagulation
cellular process
cell adhesion
Component
extracellular matrix
extracellular matrix (sensu Metazoa)
Target 7 General Function Involved in chaperone binding
Target 7 Specific Function Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site of injury, stabilizing its heterodimeric structure and protecting it from premature clearance from plasma
Target 7 Pathways Not Available
Target 7 Reactions Not Available
Target 7 Pfam Domain Function
Target 7 Signals
  • 1-22
Target 7 Transmembrane Regions
  • None
Target 7 Essentiality Non-Essential
Target 7 GenBank ID Protein 37947 Link Image
Target 7 UniProtKB/Swiss-Prot ID P04275 Link Image
Target 7 UniProtKB/Swiss-Prot Entry Name VWF_HUMAN Link Image
Target 7 PDB ID 1SQ0 Link Image
Target 7 PDB File Show
Target 7 3D Structure
Target 7 Cellular Location
  • Secreted protein. Note=Localized to storage granules
Target 7 Gene Sequence >8442 bp
ATGATTCCTGCCAGATTTGCCGGGGTGCTGCTTGCTCTGGCCCTCATTTTGCCAGGGACC
CTTTGTGCAGAAGGAACTCGCGGCAGGTCATCCACGGCCCGATGCAGCCTTTTCGGAAGT
GACTTCGTCAACACCTTTGATGGGAGCATGTACAGCTTTGCGGGATACTGCAGTTACCTC
CTGGCAGGGGGCTGCCAGAAACGCTCCTTCTCGATTATTGGGGACTTCCAGAATGGCAAG
AGAGTGAGCCTCTCCGTGTATCTTGGGGAATTTTTTGACATCCATTTGTTTGTCAATGGT
ACCGTGACACAGGGGGACCAAAGAGTCTCCATGCCCTATGCCTCCAAAGGGCTGTATCTA
GAAACTGAGGCTGGGTACTACAAGCTGTCCGGTGAGGCCTATGGCTTTGTGGCCAGGATC
GATGGCAGCGGCAACTTTCAAGTCCTGCTGTCAGACAGATACTTCAACAAGACCTGCGGG
CTGTGTGGCAACTTTAACATCTTTGCTGAAGATGACTTTATGACCCAAGAAGGGACCTTG
ACCTCGGACCCTTATGACTTTGCCAACTCATGGGCTCTGAGCAGTGGAGAACAGTGGTGT
GAACGGGCATCTCCTCCCAGCAGCTCATGCAACATCTCCTCTGGGGAAATGCAGAAGGGC
CTGTGGGAGCAGTGCCAGCTTCTGAAGAGCACCTCGGTGTTTGCCCGCTGCCACCCTCTG
GTGGACCCCGAGCCTTTTGTGGCCCTGTGTGAGAAGACTTTGTGTGAGTGTGCTGGGGGG
CTGGAGTGCGCCTGCCCTGCCCTCCTGGAGTACGCCCGGACCTGTGCCCAGGAGGGAATG
GTGCTGTACGGCTGGACCGACCACAGCGCGTGCAGCCCAGTGTGCCCTGCTGGTATGGAG
TATAGGCAGTGTGTGTCCCCTTGCGCCAGGACCTGCCAGAGCCTGCACATCAATGAAATG
TGTCAGGAGCGATGCGTGGATGGCTGCAGCTGCCCTGAGGGACAGCTCCTGGATGAAGGC
CTCTGCGTGGAGAGCACCGAGTGTCCCTGCGTGCATTCCGGAAAGCGCTACCCTCCCGGC
ACCTCCCTCTCTCGAGACTGCAACACCTGCATTTGCCGAAACAGCCAGTGGATCTGCAGC
AATGAAGAATGTCCAGGGGAGTGCCTTGTCACAGGTCAATCACACTTCAAGAGCTTTGAC
AACAGATACTTCACCTTCAGTGGGATCTGCCAGTACCTGCTGGCCCGGGATTGCCAGGAC
CACTCCTTCTCCATTGTCATTGAGACTGTCCAGTGTGCTGATGACCGCGACGCTGTGTGC
ACCCGCTCCGTCACCGTCCGGCTGCCTGGCCTGCACAACAGCCTTGTGAAACTGAAGCAT
GGGGCAGGAGTTGCCATGGATGGCCAGGACGTCCAGCTCCCCCTCCTGAAAGGTGACCTC
CGCATCCAGCATACAGTGACGGCCTCCGTGCGCCTCAGCTACGGGGAGGACCTGCAGATG
GACTGGGATGGCCGCGGGAGGCTGCTGGTGAAGCTGTCCCCCGTCTATGCCGGGAAGACC
TGCGGCCTGTGTGGGAATTACAATGGCAACCAGGGCGACGACTTCCTTACCCCCTCTGGG
CTGGCGGAGCCCCGGGTGGAGGACTTCGGGAACGCCTGGAAGCTGCACGGGGACTGCCAG
GACCTGCAGAAGCAGCACAGCGATCCCTGCGCCCTCAACCCGCGCATGACCAGGTTCTCC
GAGGAGGCGTGCGCGGTCCTGACGTCCCCCACATTCGAGGCCTGCCATCGTGCCGTCAGC
CCGCTGCCCTACCTGCGGAACTGCCGCTACGACGTGTGCTCCTGCTCGGACGGCCGCGAG
TGCCTGTGCGGCGCCCTGGCCAGCTATGCCGCGGCCTGCGCGGGGAGAGGCGTGCGCGTC
GCGTGGCGCGAGCCAGGCCGCTGTGAGCTGAACTGCCCGAAAGGCCAGGTGTACCTGCAG
TGCGGGACCCCCTGCAACCTGACCTGCCGCTCTCTCTCTTACCCGGATGAGGAATGCAAT
GAGGCCTGCCTGGAGGGCTGCTTCTGCCCCCCAGGGCTCTACATGGATGAGAGGGGGGAC
TGCGTGCCCAAGGCCCAGTGCCCCTGTTACTATGACGGTGAGATCTTCCAGCCAGAAGAC
ATCTTCTCAGACCATCACACCATGTGCTACTGTGAGGATGGCTTCATGCACTGTACCATG
AGTGGAGTCCCCGGAAGCTTGCTGCCTGACGCTGTCCTCAGCAGTCCCCTGTCTCATCGC
AGCAAAAGGAGCCTATCCTGTCGGCCCCCCATGGTCAAGCTGGTGTGTCCCGCTGACAAC
CTGCGGGCTGAAGGGCTCGAGTGTACCAAAACGTGCCAGAACTATGACCTGGAGTGCATG
AGCATGGGCTGTGTCTCTGGCTGCCTCTGCCCCCCGGGCATGGTCCGGCATGAGAACAGA
TGTGTGGCCCTGGAAAGGTGTCCCTGCTTCCATCAGGGCAAGGAGTATGCCCCTGGAGAA
ACAGTGAAGATTGGCTGCAACACTTGTGTCTGTCGGGACCGGAAGTGGAACTGCACAGAC
CATGTGTGTGATGCCACGTGCTCCACGATCGGCATGGCCCACTACCTCACCTTCGACGGG
CTCAAATACCTGTTCCCCGGGGAGTGCCAGTACGTTCTGGTGCAGGATTACTGCGGCAGT
AACCCTGGGACCTTTCGGATCCTAGTGGGGAATAAGGGATGCAGCCACCCCTCAGTGAAA
TGCAAGAAACGGGTCACCATCCTGGTGGAGGGAGGAGAGATTGAGCTGTTTGACGGGGAG
GTGAATGTGAAGAGGCCCATGAAGGATGAGACTCACTTTGAGGTGGTGGAGTCTGGCCGG
TACATCATTCTGCTGCTGGGCAAAGCCCTCTCCGTGGTCTGGGACCGCCACCTGAGCATC
TCCGTGGTCCTGAAGCAGACATACCAGGAGAAAGTGTGTGGCCTGTGTGGGAATTTTGAT
GGCATCCAGAACAATGACCTCACCAGCAGCAACCTCCAAGTGGAGGAAGACCCTGTGGAC
TTTGGGAACTCCTGGAAAGTGAGCTCGCAGTGTGCTGACACCAGAAAAGTGCCTCTGGAC
TCATCCCCTGCCACCTGCCATAACAACATCATGAAGCAGACGATGGTGGATTCCTCCTGT
AGAATCCTTACCAGTGACGTCTTCCAGGACTGCAACAAGCTGGTGGACCCCGAGCCATAT
CTGGATGTCTGCATTTACGACACCTGCTCCTGTGAGTCCATTGGGGACTGCGCCTGCTTC
TGCGACACCATTGCTGCCTATGCCCACGTGTGTGCCCAGCATGGCAAGGTGGTGACCTGG
AGGACGGCCACATTGTGCCCCCAGAGCTGCGAGGAGAGGAATCTCCGGGAGAACGGGTAT
GAGTGTGAGTGGCGCTATAACAGCTGTGCACCTGCCTGTCAAGTCACGTGTCAGCACCCT
GAGCCACTGGCCTGCCCTGTGCAGTGTGTGGAGGGCTGCCATGCCCACTGCCCTCCAGGG
AAAATCCTGGATGAGCTTTTGCAGACCTGCGTTGACCCTGAAGACTGTCCAGTGTGTGAG
GTGGCTGGCCGGCGTTTTGCCTCAGGAAAGAAAGTCACCTTGAATCCCAGTGACCCTGAG
CACTGCCAGATTTGCCACTGTGATGTTGTCAACCTCACCTGTGAAGCCTGCCAGGAGCCG
GGAGGCCTGGTGGTGCCTCCCACAGATGCCCCGGTGAGCCCCACCACTCTGTATGTGGAG
GACATCTCGGAACCGCCGTTGCACGATTTCTACTGCAGCAGGCTACTGGACCTGGTCTTC
CTGCTGGATGGCTCCTCCAGGCTGTCCGAGGCTGAGTTTGAAGTGCTGAAGGCCTTTGTG
GTGGACATGATGGAGCGGCTGCGCATCTCCCAGAAGTGGGTCCGCGTGGCCGTGGTGGAG
TACCACGACGGCTCCCACGCCTACATCGGGCTCAAGGACCGGAAGCGACCGTCAGAGCTG
CGGCGCATTGCCAGCCAGGTGAAGTATGCGGGCAGCCAGGTGGCCTCCACCAGCGAGGTC
TTGAAATACACACTGTTCCAAATCTTCAGCAAGATCGACCGCCCTGAAGCCTCCCGCATC
GCCCTGCTCCTGATGGCCAGCCAGGAGCCCCAACGGATGTCCCGGAACTTTGTCCGCTAC
GTCCAGGGCCTGAAGAAGAAGAAGGTCATTGTGATCCCGGTGGGCATTGGGCCCCATGCC
AACCTCAAGCAGATCCGCCTCATCGAGAAGCAGGCCCCTGAGAACAAGGCCTTCGTGCTG
AGCAGTGTGGATGAGCTGGAGCAGCAAAGGGACGAGATCGTTAGCTACCTCTGTGACCTT
GCCCCTGAAGCCCCTCCTCCTACTCTGCCCCCCCACATGGCACAAGTCACTGTGGGCCCG
GGGCTCTTGGGGGTTTCGACCCTGGGGCCCAAGAGGAACTCCATGGTTCTGGATGTGGCG
TTCGTCCTGGAAGGATCGGACAAAATTGGTGAAGCCGACTTCAACAGGAGCAAGGAGTTC
ATGGAGGAGGTGATTCAGCGGATGGATGTGGGCCAGGACAGCATCCACGTCACGGTGCTG
CAGTACTCCTACATGGTGACCGTGGAGTACCCCTTCAGCGAGGCACAGTCCAAAGGGGAC
ATCCTGCAGCGGGTGCGAGAGATCCGCTACCAGGGCGGCAACAGGACCAACACTGGGCTG
GCCCTGCGGTACCTCTCTGACCACAGCTTCTTGGTCAGCCAGGGTGACCGGGAGCAGGCG
CCCAACCTGGTCTACATGGTCACCGGAAATCCTGCCTCTGATGAGATCAAGAGGCTGCCT
GGAGACATCCAGGTGGTGCCCATTGGAGTGGGCCCTAATGCCAACGTGCAGGAGCTGGAG
AGGATTGGCTGGCCCAATGCCCCTATCCTCATCCAGGACTTTGAGACGCTCCCCCGAGAG
GCTCCTGACCTGGTGCTGCAGAGGTGCTGCTCCGGAGAGGGGCTGCAGATCCCCACCCTC
TCCCCTGCACCTGACTGCAGCCAGCCCCTGGACGTGATCCTTCTCCTGGATGGCTCCTCC
AGTTTCCCAGCTTCTTATTTTGATGAAATGAAGAGTTTCGCCAAGGCTTTCATTTCAAAA
GCCAATATAGGGCCTCGTCTCACTCAGGTGTCAGTGCTGCAGTATGGAAGCATCACCACC
ATTGACGTGCCATGGAACGTGGTCCCGGAGAAAGCCCATTTGCTGAGCCTTGTGGACGTC
ATGCAGCGGGAGGGAGGCCCCAGCCAAATCGGGGATGCCTTGGGCTTTGCTGTGCGATAC
TTGACTTCAGAAATGCATGGTGCCAGGCCGGGAGCCTCAAAGGCGGTGGTCATCCTGGTC
ACGGACGTCTCTGTGGATTCAGTGGATGCAGCAGCTGATGCCGCCAGGTCCAACAGAGTG
ACAGTGTTCCCTATTGGAATTGGAGATCGCTACGATGCAGCCCAGCTACGGATCTTGGCA
GGCCCAGCAGGCGACTCCAACGTGGTGAAGCTCCAGCGAATCGAAGACCTCCCTACCATG
GTCACCTTGGGCAATTCCTTCCTCCACAAACTGTGCTCTGGATTTGTTAGGATTTGCATG
GATGAGGATGGGAATGAGAAGAGGCCCGGGGACGTCTGGACCTTGCCAGACCAGTGCCAC
ACCGTGACTTGCCAGCCAGATGGCCAGACCTTGCTGAAGACTCATCGGGTCAACTGTGAC
CGGGGGCTGAGGCCTTCGTGCCCTAACAGCCAGTCCCCTGTTAAAGTGGAAGAGACCTGT
GGCTGCCGCTGGACCTGCCCCTGCGTGTGCACAGGCAGCTCCACTCGGCACATCGTGACC
TTTGATGGGCAGAATTTCAAGCTGACTGGCAGCTGTTCTTATGTCCTATTTCAAAACAAG
GAGCAGGACCTGGAGGTGATTCTCCATAATGGTGCCTGCAGCCCTGGAGCAAGGCAGGGC
TGCATGAAATCCATCGAGGTGAAGCACAGTGCCCTCTCCGTCGAGCTGCACAGTGACATG
GAGGTGACGGTGAATGGGAGACTGGTCTCTGTTCCTTACGTGGGTGGGAACATGGAAGTC
AACGTTTATGGTGCCATCATGCATGAGGTCAGATTCAATCACCTTGGTCACATCTTCACA
TTCACTCCACAAAACAATGAGTTCCAACTGCAGCTCAGCCCCAAGACTTTTGCTTCAAAG
ACGTATGGTCTGTGTGGGATCTGTGATGAGAACGGAGCCAATGACTTCATGCTGAGGGAT
GGCACAGTCACCACAGACTGGAAAACACTTGTTCAGGAATGGACTGTGCAGCGGCCAGGG
CAGACGTGCCAGCCCATCCTGGAGGAGCAGTGTCTTGTCCCCGACAGCTCCCACTGCCAG
GTCCTCCTCTTACCACTGTTTGCTGAATGCCACAAGGTCCTGGCTCCAGCCACATTCTAT
GCCATCTGCCAGCAGGACAGTTGCCACCAGGAGCAAGTGTGTGAGGTGATCGCCTCTTAT
GCCCACCTCTGTCGGACCAACGGGGTCTGCGTTGACTGGAGGACACCTGATTTCTGTGCT
ATGTCATGCCCACCATCTCTGGTCTACAACCACTGTGAGCATGGCTGTCCCCGGCACTGT
GATGGCAACGTGAGCTCCTGTGGGGACCATCCCTCCGAAGGCTGTTTCTGCCCTCCAGAT
AAAGTCATGTTGGAAGGCAGCTGTGTCCCTGAAGAGGCCTGCACTCAGTGCATTGGTGAG
GATGGAGTCCAGCACCAGTTCCTGGAAGCCTGGGTCCCGGACCACCAGCCCTGTCAGATC
TGCACATGCCTCAGCGGGCGGAAGGTCAACTGCACAACGCAGCCCTGCCCCACGGCCAAA
GCTCCCACGTGTGGCCTGTGTGAAGTAGCCCGCCTCCGCCAGAATGCAGACCAGTGCTGC
CCCGAGTATGAGTGTGTGTGTGACCCAGTGAGCTGTGACCTGCCCCCAGTGCCTCACTGT
GAACGTGGCCTCCAGCCCACACTGACCAACCCTGGCGAGTGCAGACCCAACTTCACCTGC
GCCTGCAGGAAGGAGGAGTGCAAAAGAGTGTCCCCACCCTCCTGCCCCCCGCACCGTTTG
CCCACCCTTCGGAAGACCCAGTGCTGTGATGAGTATGAGTGTGCCTGCAACTGTGTCAAC
TCCACAGTGAGCTGTCCCCTTGGGTACTTGGCCTCAACCGCCACCAATGACTGTGGCTGT
ACCACAACCACCTGCCTTCCCGACAAGGTGTGTGTCCACCGAAGCACCATCTACCCTGTG
GGCCAGTTCTGGGAGGAGGGCTGCGATGTGTGCACCTGCACCGACATGGAGGATGCCGTG
ATGGGCCTCCGCGTGGCCCAGTGCTCCCAGAAGCCCTGTGAGGACAGCTGTCGGTCGGGC
TTCACTTACGTTCTGCATGAAGGCGAGTGCTGTGGAAGGTGCCTGCCATCTGCCTGTGAG
GTGGTGACTGGCTCACCGCGGGGGGACTCCCAGTCTTCCTGGAAGAGTGTCGGCTCCCAG
TGGGCCTCCCCGGAGAACCCCTGCCTCATCAATGAGTGTGTCCGAGTGAAGGAGGAGGTC
TTTATACAACAAAGGAACGTCTCCTGCCCCCAGCTGGAGGTCCCTGTCTGCCCCTCGGGC
TTTCAGCTGAGCTGTAAGACCTCAGCGTGCTGCCCAAGCTGTCGCTGTGAGCGCATGGAG
GCCTGCATGCTCAATGGCACTGTCATTGGGCCCGGGAAGACTGTGATGATCGATGTGTGC
ACGACCTGCCGCTGCATGGTGCAGGTGGGGGTCATCTCTGGATTCAAGCTGGAGTGCAGG
AAGACCACCTGCAACCCCTGCCCCCTGGGTTACAAGGAAGAAAATAACACAGGTGAATGT
TGTGGGAGATGTTTGCCTACGGCTTGCACCATTCAGCTAAGAGGAGGACAGATCATGACA
CTGAAGCGTGATGAGACGCTCCAGGATGGCTGTGATACTCACTTCTGCAAGGTCAATGAG
AGAGGAGAGTACTTCTGGGAGAAGAGGGTCACAGGCTGCCCACCCTTTGATGAACACAAG
TGTCTGGCTGAGGGAGGTAAAATTATGAAAATTCCAGGCACCTGCTGTGACACATGTGAG
GAGCCTGAGTGCAACGACATCACTGCCAGGCTGCAGTATGTCAAGGTGGGAAGCTGTAAG
TCTGAAGTAGAGGTGGATATCCACTACTGCCAGGGCAAATGTGCCAGCAAAGCCATGTAC
TCCATTGACATCAACGATGTGCAGGACCAGTGCTCCTGCTGCTCTCCGACACGGACGGAG
CCCATGCAGGTGGCCCTGCACTGCACCAATGGCTCTGTTGTGTACCATGAGGTTCTCAAT
GCCATGGAGTGCAAATGCTCCCCCAGGAAGTGCAGCAAGTGA
Target 7 GenBank Gene ID
Target 7 GeneCard ID VWF Link Image
Target 7 GenAtlas ID VWF Link Image
Target 7 HGNC ID HGNC:12726 Link Image
Target 7 Chromosome Location 12
Target 7 Locus 12p13.3
Target 7 SNPs SNPJam Report Link Image
Target 7 General References
  1. Allen S, Abuzenadah AM, Hinks J, Blagg JL, Gursel T, Ingerslev J, Goodeve AC, Peake IR, Daly ME: A novel von Willebrand disease-causing mutation (Arg273Trp) in the von Willebrand factor propeptide that results in defective multimerization and secretion. Blood. 2000 Jul 15;96(2):560-8. [PubMed Link Image]
  2. Haberichter SL, Fahs SA, Montgomery RR: von Willebrand factor storage and multimerization: 2 independent intracellular processes. Blood. 2000 Sep 1;96(5):1808-15. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Ruggeri ZM: Von Willebrand factor, platelets and endothelial cell interactions. J Thromb Haemost. 2003 Jul;1(7):1335-42. [PubMed Link Image]
  5. Rabinowitz I, Tuley EA, Mancuso DJ, Randi AM, Firkin BG, Howard MA, Sadler JE: von Willebrand disease type B: a missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9846-9. [PubMed Link Image]
  6. Donner M, Kristoffersson AC, Lenk H, Scheibel E, Dahlback B, Nilsson IM, Holmberg L: Type IIB von Willebrand's disease: gene mutations and clinical presentation in nine families from Denmark, Germany and Sweden. Br J Haematol. 1992 Sep;82(1):58-65. [PubMed Link Image]
  7. Lavergne JM, De Paillette L, Bahnak BR, Ribba AS, Fressinaud E, Meyer D, Pietu G: Defects in type IIA von Willebrand disease: a cysteine 509 to arginine substitution in the mature von Willebrand factor disrupts a disulphide loop involved in the interaction with platelet glycoprotein Ib-IX. Br J Haematol. 1992 Sep;82(1):66-72. [PubMed Link Image]
  8. Pietu G, Ribba AS, de Paillette L, Cherel G, Lavergne JM, Bahnak BR, Meyer D: Molecular study of von Willebrand disease: identification of potential mutations in patients with type IIA and type IIB. Blood Coagul Fibrinolysis. 1992 Aug;3(4):415-21. [PubMed Link Image]
  9. Ribba AS, Voorberg J, Meyer D, Pannekoek H, Pietu G: Characterization of recombinant von Willebrand factor corresponding to mutations in type IIA and type IIB von Willebrand disease. J Biol Chem. 1992 Nov 15;267(32):23209-15. [PubMed Link Image]
  10. Cooney KA, Nichols WC, Bruck ME, Bahou WF, Shapiro AD, Bowie EJ, Gralnick HR, Ginsburg D: The molecular defect in type IIB von Willebrand disease. Identification of four potential missense mutations within the putative GpIb binding domain. J Clin Invest. 1991 Apr;87(4):1227-33. [PubMed Link Image]
  11. 1673047 Iannuzzi MC, Hidaka N, Boehnke M, Bruck ME, Hanna WT, Collins FS, Ginsburg D: Analysis of the relationship of von Willebrand disease (vWD) and hereditary hemorrhagic telangiectasia and identification of a potential type IIA vWD mutation (IIe865 to Thr). Am J Hum Genet. 1991 Apr;48(4):757-63.
  12. 1729889 Murray EW, Giles AR, Lillicrap D: Germ-line mosaicism for a valine-to-methionine substitution at residue 553 in the glycoprotein Ib-binding domain of von Willebrand factor, causing type IIB von Willebrand disease. Am J Hum Genet. 1992 Jan;50(1):199-207.
  13. 1761120 Donner M, Andersson AM, Kristoffersson AC, Nilsson IM, Dahlback B, Holmberg L: An Arg545----Cys545 substitution mutation of the von Willebrand factor in type IIB von Willebrand's disease. Eur J Haematol. 1991 Nov;47(5):342-5.
  14. 1832934 Gaucher C, Mercier B, Jorieux S, Oufkir D, Mazurier C: Identification of two point mutations in the von Willebrand factor gene of three families with the 'Normandy' variant of von Willebrand disease. Br J Haematol. 1991 Aug;78(4):506-14.
  15. 1906179 Tuley EA, Gaucher C, Jorieux S, Worrall NK, Sadler JE, Mazurier C: Expression of von Willebrand factor "Normandy": an autosomal mutation that mimics hemophilia A. Proc Natl Acad Sci U S A. 1991 Jul 15;88(14):6377-81.
  16. 1988024 Mancuso DJ, Tuley EA, Westfield LA, Lester-Mancuso TL, Le Beau MM, Sorace JM, Sadler JE: Human von Willebrand factor gene and pseudogene: structural analysis and differentiation by polymerase chain reaction. Biochemistry. 1991 Jan 8;30(1):253-69.
  17. 2010538 Randi AM, Rabinowitz I, Mancuso DJ, Mannucci PM, Sadler JE: Molecular basis of von Willebrand disease type IIB. Candidate mutations cluster in one disulfide loop between proposed platelet glycoprotein Ib binding sequences. J Clin Invest. 1991 Apr;87(4):1220-6.
  18. 2011604 Ware J, Dent JA, Azuma H, Sugimoto M, Kyrle PA, Yoshioka A, Ruggeri ZM: Identification of a point mutation in type IIB von Willebrand disease illustrating the regulation of von Willebrand factor affinity for the platelet membrane glycoprotein Ib-IX receptor. Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2946-50.
  19. 2584182 Mancuso DJ, Tuley EA, Westfield LA, Worrall NK, Shelton-Inloes BB, Sorace JM, Alevy YG, Sadler JE: Structure of the gene for human von Willebrand factor. J Biol Chem. 1989 Nov 25;264(33):19514-27.
  20. 2786201 Ginsburg D, Konkle BA, Gill JC, Montgomery RR, Bockenstedt PL, Johnson TA, Yang AY: Molecular basis of human von Willebrand disease: analysis of platelet von Willebrand factor mRNA. Proc Natl Acad Sci U S A. 1989 May;86(10):3723-7.
  21. 2828057 Bonthron D, Orkin SH: The human von Willebrand factor gene. Structure of the 5' region. Eur J Biochem. 1988 Jan 15;171(1-2):51-7.
  22. 2864688 Sadler JE, Shelton-Inloes BB, Sorace JM, Harlan JM, Titani K, Davie EW: Cloning and characterization of two cDNAs coding for human von Willebrand factor. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6394-8.
  23. 3019665 Verweij CL, Diergaarde PJ, Hart M, Pannekoek H: Full-length von Willebrand factor (vWF) cDNA encodes a highly repetitive protein considerably larger than the mature vWF subunit. EMBO J. 1986 Aug;5(8):1839-47.
  24. 3089784 Samor B, Michalski JC, Debray H, Mazurier C, Goudemand M, Van Halbeek H, Vliegenthart JF, Montreuil J: Primary structure of a new tetraantennary glycan of the N-acetyllactosaminic type isolated from human factor VIII/von Willebrand factor. Eur J Biochem. 1986 Jul 15;158(2):295-8.
  25. 3488076 Shelton-Inloes BB, Titani K, Sadler JE: cDNA sequences for human von Willebrand factor reveal five types of repeated domains and five possible protein sequence polymorphisms. Biochemistry. 1986 Jun 3;25(11):3164-71.
  26. 3489923 Bonthron D, Orr EC, Mitsock LM, Ginsburg D, Handin RI, Orkin SH: Nucleotide sequence of pre-pro-von Willebrand factor cDNA. Nucleic Acids Res. 1986 Sep 11;14(17):7125-7.
  27. 3495266 Shelton-Inloes BB, Broze GJ Jr, Miletich JP, Sadler JE: Evolution of human von Willebrand factor: cDNA sequence polymorphisms, repeated domains, and relationship to von Willebrand antigen II. Biochem Biophys Res Commun. 1987 Apr 29;144(2):657-65.
  28. 3496594 Collins CJ, Underdahl JP, Levene RB, Ravera CP, Morin MJ, Dombalagian MJ, Ricca G, Livingston DM, Lynch DC: Molecular cloning of the human gene for von Willebrand factor and identification of the transcription initiation site. Proc Natl Acad Sci U S A. 1987 Jul;84(13):4393-7.
  29. 3502076 Marti T, Rosselet SJ, Titani K, Walsh KA: Identification of disulfide-bridged substructures within human von Willebrand factor. Biochemistry. 1987 Dec 15;26(25):8099-109.
  30. 3524673 Titani K, Kumar S, Takio K, Ericsson LH, Wade RD, Ashida K, Walsh KA, Chopek MW, Sadler JE, Fujikawa K: Amino acid sequence of human von Willebrand factor. Biochemistry. 1986 Jun 3;25(11):3171-84.
  31. 3873280 Lynch DC, Zimmerman TS, Collins CJ, Brown M, Morin MJ, Ling EH, Livingston DM: Molecular cloning of cDNA for human von Willebrand factor: authentication by a new method. Cell. 1985 May;41(1):49-56.
  32. 3874428 Ginsburg D, Handin RI, Bonthron DT, Donlon TA, Bruns GA, Latt SA, Orkin SH: Human von Willebrand factor (vWF): isolation of complementary DNA (cDNA) clones and chromosomal localization. Science. 1985 Jun 21;228(4706):1401-6.
  33. 3875078 Verweij CL, de Vries CJ, Distel B, van Zonneveld AJ, van Kessel AG, van Mourik JA, Pannekoek H: Construction of cDNA coding for human von Willebrand factor using antibody probes for colony-screening and mapping of the chromosomal gene. Nucleic Acids Res. 1985 Jul 11;13(13):4699-717.
  34. 7620154 Hilbert L, Gaucher C, Mazurier C: Identification of two mutations (Arg611Cys and Arg611His) in the A1 loop of von Willebrand factor (vWF) responsible for type 2 von Willebrand disease with decreased platelet-dependent function of vWF. Blood. 1995 Aug 1;86(3):1010-8.
  35. 7734373 Castaman G, Eikenboom JC, Rodeghiero F, Briet E, Reitsma PH: A novel candidate mutation (Arg611-->His) in type I 'platelet discordant' von Willebrand's disease with desmopressin-induced thrombocytopenia. Br J Haematol. 1995 Mar;89(3):656-8.
  36. 7789955 Schneppenheim R, Thomas KB, Krey S, Budde U, Jessat U, Sutor AH, Zieger B: Identification of a candidate missense mutation in a family with von Willebrand disease type IIC. Hum Genet. 1995 Jun;95(6):681-6.
  37. 7989040 Schneppenheim R, Krey S, Bergmann F, Bock D, Budde U, Lange M, Linde R, Mittler U, Meili E, Mertes G, et al.: Genetic heterogeneity of severe von Willebrand disease type III in the German population. Hum Genet. 1994 Dec;94(6):640-52.
  38. 8011991 Uno H, Nishida N, Ishizaki J, Suzuki M, Nishikubo T, Miyata S, Takahashi Y, Yoshioka A, Tsuda K: Investigation of type IIC von Willebrand disease. Int J Hematol. 1994 Apr;59(3):219-25.
  39. 8088787 Zhang ZP, Blomback M, Egberg N, Falk G, Anvret M: Characterization of the von Willebrand factor gene (VWF) in von Willebrand disease type III patients from 24 families of Swedish and Finnish origin. Genomics. 1994 May 1;21(1):188-93.
  40. 8123843 Hilbert L, Gaucher C, de Romeuf C, Horellou MH, Vink T, Mazurier C: Leu 697-->Val mutation in mature von Willebrand factor is responsible for type IIB von Willebrand disease. Blood. 1994 Mar 15;83(6):1542-50.
  41. 8123844 Lyons SE, Cooney KA, Bockenstedt P, Ginsburg D: Characterization of Leu777Pro and Ile865Thr type IIA von Willebrand disease mutations. Blood. 1994 Mar 15;83(6):1551-7.
  42. 8338947 Inbal A, Englender T, Kornbrot N, Randi AM, Castaman G, Mannucci PM, Sadler JE: Identification of three candidate mutations causing type IIA von Willebrand disease using a rapid, nonradioactive, allele-specific hybridization method. Blood. 1993 Aug 1;82(3):830-6.
  43. 8348943 Donner M, Kristoffersson AC, Berntorp E, Scheibel E, Thorsen S, Dahlback B, Nilsson IM, Holmberg L: Two new candidate mutations in type IIA von Willebrand's disease (Arg834-->Gly, Gly846-->Arg) and one polymorphism (Tyr821-->Cys) in the A2 region of the von Willebrand factor. Eur J Haematol. 1993 Jul;51(1):38-44.
  44. 8376405 Rabinowitz I, Randi AM, Shindler KS, Tuley EA, Rustagi PK, Sadler JE: Type IIB mutation His-505-->Asp implicates a new segment in the control of von Willebrand factor binding to platelet glycoprotein Ib. J Biol Chem. 1993 Sep 25;268(27):20497-501.
  45. 8435341 Gaucher C, Hanss M, Dechavanne M, Mazurier C: Substitution of cysteine for phenylalanine 751 in mature von Willebrand factor is a novel candidate mutation in a family with type IIA von Willebrand disease. Br J Haematol. 1993 Jan;83(1):94-9.
  46. 8486782 Holmberg L, Dent JA, Schneppenheim R, Budde U, Ware J, Ruggeri ZM: von Willebrand factor mutation enhancing interaction with platelets in patients with normal multimeric structure. J Clin Invest. 1993 May;91(5):2169-77.
  47. 8547152 Hilbert L, Gaucher C, Mazurier C: Effects of different amino-acid substitutions in the leucine 694-proline 708 segment of recombinant von Willebrand factor. Br J Haematol. 1995 Dec;91(4):983-90.
  48. 8622978 Schneppenheim R, Brassard J, Krey S, Budde U, Kunicki TJ, Holmberg L, Ware J, Ruggeri ZM: Defective dimerization of von Willebrand factor subunits due to a Cys-> Arg mutation in type IID von Willebrand disease. Proc Natl Acad Sci U S A. 1996 Apr 16;93(8):3581-6.
  49. 9312128 Bienkowska J, Cruz M, Atiemo A, Handin R, Liddington R: The von willebrand factor A3 domain does not contain a metal ion-dependent adhesion site motif. J Biol Chem. 1997 Oct 3;272(40):25162-7.
  50. 9331419 Huizinga EG, Martijn van der Plas R, Kroon J, Sixma JJ, Gros P: Crystal structure of the A3 domain of human von Willebrand factor: implications for collagen binding. Structure. 1997 Sep 15;5(9):1147-56.
  51. 9553097 Emsley J, Cruz M, Handin R, Liddington R: Crystal structure of the von Willebrand Factor A1 domain and implications for the binding of platelet glycoprotein Ib. J Biol Chem. 1998 Apr 24;273(17):10396-401.
Target 7 Drug References
  1. Shord SS, Lindley CM: Coagulation products and their uses. Am J Health Syst Pharm. 2000 Aug 1;57(15):1403-17; quiz 1418-20. [PubMed Link Image]
  2. Lillicrap D, Poon MC, Walker I, Xie F, Schwartz BA: Efficacy and safety of the factor VIII/von Willebrand factor concentrate, haemate-P/humate-P: ristocetin cofactor unit dosing in patients with von Willebrand disease. Thromb Haemost. 2002 Feb;87(2):224-30. [PubMed Link Image]
  3. Gill JC, Ewenstein BM, Thompson AR, Mueller-Velten G, Schwartz BA: Successful treatment of urgent bleeding in von Willebrand disease with factor VIII/VWF concentrate (Humate-P): use of the ristocetin cofactor assay (VWF:RCo) to measure potency and to guide therapy. Haemophilia. 2003 Nov;9(6):688-95. [PubMed Link Image]
  4. Smith KJ, Lusher JM, Cohen AR, Salzman P: Initial clinical experience with a new pasteurized monoclonal antibody purified factor VIIIC. Semin Hematol. 1990 Apr;27(2 Suppl 2):25-9. [PubMed Link Image]
  5. Altieri DC, Capitanio AM, Mannucci PM: von Willebrand factor contaminating porcine factor VIII concentrate (Hyate:C) causes platelet aggregation. Br J Haematol. 1986 Aug;63(4):703-11. [PubMed Link Image]
Drug Target 8 [top]
Target 8 ID 1847
Target 8 Name 78 kDa glucose-regulated protein
Target 8 Synonyms
  1. 78 kDa glucose-regulated protein precursor
  2. BiP
  3. Endoplasmic reticulum lumenal Ca(2+)-binding protein grp78
  4. GRP 78
  5. Heat shock 70 kDa protein 5
  6. Immunoglobulin heavy chain-binding protein
Target 8 Gene Name HSPA5
Target 8 Protein Sequence >78 kDa glucose-regulated protein precursor
MKLSLVAAMLLLLSAARAEEEDKKEDVGTVVGIDLGTTYSCVGVFKNGRVEIIANDQGNR
ITPSYVAFTPEGERLIGDAAKNQLTSNPENTVFDAKRLIGRTWNDPSVQQDIKFLPFKVV
EKKTKPYIQVDIGGGQTKTFAPEEISAMVLTKMKETAEAYLGKKVTHAVVTVPAYFNDAQ
RQATKDAGTIAGLNVMRIINEPTAAAIAYGLDKREGEKNILVFDLGGGTFDVSLLTIDNG
VFEVVATNGDTHLGGEDFDQRVMEHFIKLYKKKTGKDVRKDNRAVQKLRREVEKAKRALS
SQHQARIEIESFYEGEDFSETLTRAKFEELNMDLFRSTMKPVQKVLEDSDLKKSDIDEIV
LVGGSTRIPKIQQLVKEFFNGKEPSRGINPDEAVAYGAAVQAGVLSGDQDTGDLVLLDVC
PLTLGIETVGGVMTKLIPRNTVVPTKKSQIFSTASDNQPTVTIKVYEGERPLTKDNHLLG
TFDLTGIPPAPRGVPQIEVTFEIDVNGILRVTAEDKGTGNKNKITITNDQNRLTPEEIER
MVNDAEKFAEEDKKLKERIDTRNELESYAYSLKNQIGDKEKLGGKLSSEDKETMEKAVEE
KIEWLESHQDADIEDFKAKKKELEEIVQPIISKLYGSAGPPPTGEEDTAEKDEL
Target 8 Number of Residues 664
Target 8 Molecular Weight 72334
Target 8 Theoretical pI 4.80
Target 8 GO Classification
Function
binding
nucleotide binding
purine nucleotide binding
adenyl nucleotide binding
ATP binding
Process
Not Available
Component
Not Available
Target 8 General Function Posttranslational modification, protein turnover, chaperones
Target 8 Specific Function Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER
Target 8 Pathways Not Available
Target 8 Reactions Not Available
Target 8 Pfam Domain Function
Target 8 Signals
  • 1-18
Target 8 Transmembrane Regions
  • None
Target 8 Essentiality Non-Essential
Target 8 GenBank ID Protein 386758 Link Image
Target 8 UniProtKB/Swiss-Prot ID P11021 Link Image
Target 8 UniProtKB/Swiss-Prot Entry Name GRP78_HUMAN Link Image
Target 8 PDB ID Not Available
Target 8 Cellular Location
  • Endoplasmic reticulum
  • endoplasmic reticulum lumen. Melanosome. Note=Identified by mass spectrometry
Target 8 Gene Sequence >1962 bp
ATGAAGCTCTCCCTGGTGGCCGCGATGCTGCTGCTGCTCAGCGCGGCGCGGGCCGAGGAG
GAGGACAAGAAGGAGGACGTGGGCACGGTGGTCGGCATCGACTTGGGGACCACCTACTCC
TGCGTCGGCGTGTTCAAGAACGGCCGCGTGGAGATCATCGCCAACGATCAGGGCAACCGC
ATCACGCCGTCCTATGTCGCCTTCACTCCTGAAGGGGAACGTCTGATTGGCGATGCCGCC
AAGAACCAGCTCACCTCCAACCCCGAGAACACGGTCTTTGACGCCAAGCGGCTCATCGGC
CGCACGTGGAATGACCCGTCTGTGCAGCAGGACATCAAGTTCTTGCCGTTCAAGGTGGTT
GAAAAGAAAACTAAACCATACATTCAAGTTGATATTGGAGGTGGGCAAACAAAGACATTT
GCTCCTGAAGAAATTTCTGCCATGGTTCTCACTAAAATGAAAGAAACCGCTGAGGCTTAT
TTGGGAAAGAAGGTTACCCATGCAGTTGTTACTGTACCAGCCTATTTTAATGATGCCCAA
CGCCAAGCAACCAAAGACGCTGGAACTATTGCTGGCCTAAATGTTATGAGGATCATCAAC
GAGCCTACGGCAGCTGCTATTGCTTATGGCCTGGATAAGAGGGAGGGGGAGAAGAACATC
CTGGTGTTTGACCTGGGTGGCGGAACCTTCGATGTGTCTCTTCTCACCATTGACAATGGT
GTCTTCGAAGTTGTGGCCACTAATGGAGATACTCATCTGGGTGGAGAAGACTTTGACCAG
CGTGTCATGGAACACTTCATCAAACTGTACAAAAAGAAGACGGGCAAAGATGTCAGGAAG
GACAATAGAGCTGTGCAGAAACTCCGGCGCGAGGTAGAAAAGGCCAAGGCCCTGTCTTCT
CAGCATCAAGCAAGAATTGAAATTGAGTCCTTCTATGAAGGAGAAGACTTTTCTGAGACC
CTGACTCGGGCCAAATTTGAAGAGCTCAACATGGATCTGTTCCGGTCTACTATGAAGCCC
GTCCAGAAAGTGTTGGAAGATTCTGATTTGAAGAAGTCTGATATTGATGAAATTGTTCTT
GTTGGTGGCTCGACTCGAATTCCAAAGATTCAGCAACTGGTTAAAGAGTTCTTCAATGGC
AAGGAACCATCCCGTGGCATAAACCCAGATGAAGCTGTAGCGTATGGTGCTGCTGTCCAG
GCTGGTGTGCTCTCTGGTGATCAAGATACAGGTGACCTGGTACTGCTTCATGTATGTCCC
CTTACACTTGGTATTGAAACTGTAGGAGGTGTCATGACCAAACTGATTCCAAGTAATACA
GTGGTGCCTACCAAGAACTCTCAGATCTTTTCTACAGCTTCTGATAATCAACCAACTGTT
ACAATCAAGGTCTATGAAGGTGAAAGACCCCTGACAAAAGACAATCATCTTCTGGGTACA
TTTGATCTGACTGGAATTCCTCCTGCTCCTCGTGGGGTCCCACAGATTGAAGTCACCTTT
GAGATAGATGTGAATGGTATTCTTCGAGTGACAGCTGAAGACAAGGGTACAGGGAACAAA
AATAAGATCACAATCACCAATGACCAGAATCGCCTGACACCTGAAGAAATCGAAAGGATG
GTTAATGATGCTGAGAAGTTTGCTGAGGAAGACAAAAAGCTGAAGGAGCGCATTGATACT
AGAAATGAGTTGGAAAGCTATGCCTATTCTCTAAAGAATCAGATTGGAGATAAAGAAAAG
CTGGGAGGTAAACTTTCCTCTGAAGATAAGGAGACCATGGAAAAAGCTGTAGAAGAAAAG
ATTGAATGGCTGGAAAGCCACCAAGATGCTGACATTGAAGACTTCAAAGCTAAGAAGAAG
GAACTGGAAGAAATTGTTCAACCAATTATCAGCAAACTCTATGGAAGTGCAGGCCCTCCC
CCAACTGGTGAAGAGGATACAGCAGAAAAAGATGAGTTGTAG
Target 8 GenBank Gene ID
Target 8 GeneCard ID HSPA5 Link Image
Target 8 GenAtlas ID HSPA5 Link Image
Target 8 HGNC ID HGNC:5238 Link Image
Target 8 Chromosome Location 9
Target 8 Locus 9q33-q34.1
Target 8 SNPs SNPJam Report Link Image
Target 8 General References
  1. Chao CC, Lin-Chao S: A direct-repeat sequence of the human BiP gene is required for A23187-mediated inducibility and an inducible nuclear factor binding. Nucleic Acids Res. 1992 Dec 25;20(24):6481-5. [PubMed Link Image]
  2. Dana RC, Welch WJ, Deftos LJ: Heat shock proteins bind calcitonin. Endocrinology. 1990 Jan;126(1):672-4. [PubMed Link Image]
  3. Ting J, Lee AS: Human gene encoding the 78,000-dalton glucose-regulated protein and its pseudogene: structure, conservation, and regulation. DNA. 1988 May;7(4):275-86. [PubMed Link Image]
  4. Rasmussen RK, Ji H, Eddes JS, Moritz RL, Reid GE, Simpson RJ, Dorow DS: Two-dimensional electrophoretic analysis of human breast carcinoma proteins: mapping of proteins that bind to the SH3 domain of mixed lineage kinase MLK2. Electrophoresis. 1997 Mar-Apr;18(3-4):588-98. [PubMed Link Image]
  5. Ji H, Reid GE, Moritz RL, Eddes JS, Burgess AW, Simpson RJ: A two-dimensional gel database of human colon carcinoma proteins. Electrophoresis. 1997 Mar-Apr;18(3-4):605-13. [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 3830
Target 9 Name Calreticulin
Target 9 Synonyms
  1. CRP55
  2. Calregulin
  3. Calreticulin precursor
  4. ERp60
  5. HACBP
  6. grp60
Target 9 Gene Name CALR
Target 9 Protein Sequence >Calreticulin
MLLSVPLLLGLLGLAVAEPAVYFKEQFLDGDGWTSRWIESKHKSDFGKFVLSSGKFYGDE
EKDKGLQTSQDARFYALSASFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPNSLDQT
DMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDN
TYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPE
HIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYS
PDPSIYAYDNFGVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDK
QDEEQRLKEEEEDKKRKEEEEAEDKEDDEDKDEDEEDEEDKEEDEEEDVPGQAKDEL
Target 9 Number of Residues 423
Target 9 Molecular Weight 48142
Target 9 Theoretical pI 4.04
Target 9 GO Classification
Function
protein binding
unfolded protein binding
binding
ion binding
cation binding
calcium ion binding
Process
physiological process
metabolism
macromolecule metabolism
protein metabolism
cellular protein metabolism
protein folding
Component
organelle
membrane-bound organelle
intracellular membrane-bound organelle
endoplasmic reticulum
Target 9 General Function Not Available
Target 9 Specific Function Molecular calcium binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export
Target 9 Pathways Not Available
Target 9 Reactions Not Available
Target 9 Pfam Domain Function
Target 9 Signals
  • 1-17
Target 9 Transmembrane Regions
  • None
Target 9 Essentiality Non-Essential
Target 9 GenBank ID Protein 337487 Link Image
Target 9 UniProtKB/Swiss-Prot ID P27797 Link Image
Target 9 UniProtKB/Swiss-Prot Entry Name CALR_HUMAN Link Image
Target 9 PDB ID Not Available
Target 9 Cellular Location
  • Endoplasmic reticulum
Target 9 Gene Sequence >1254 bp
ATGCTGCTATCCGTGCCGCTGCTGCTCGGCCTCCTCGGCCTGGCCGTCGCCGAGCCCGCC
GTCTACTTCAAGGAGCAGTTTCTGGACGGAGACGGGTGGACTTCCCGCTGGATCGAATCC
AAACACAAGTCAGATTTTGGCAAATTCGTTCTCAGTTCCGGCAAGTTCTACGGTGACGAG
GAGAAAGATAAAGGTTTGCAGACAAGCCAGGATGCACGCTTTTATGCTCTGTCGGCCAGT
TTCGAGCCTTTCAGCAACAAAGGCCAGACGCTGGTGGTGCAGTTCACGGTGAAACATGAG
CAGAACATCGACTGTGGGGGCGGCTATGTGAAGCTGTTTCCTAATAGTTTGGACCAGACA
GACATGCACGGAGACTCAGAATACAACATCATGTTTGGTCCCGACATCTGTGGCCCTGGC
ACCAAGAAGGTTCATGTCATCTTCAACTACAAGGGCAAGAACGTGCTGATCAACAAGGAC
ATCCGTTGCAAGGATGATGAGTTTACACACCTGTACACACTGATTGTGCGGCCAGACAAC
ACCTATGAGGTGAAGATTGACAACAGCCAGGTGGAGTCCGGCTCCTTGGAAGACGATTGG
GACTTCCTGCCACCCAAGAAGATAAAGGATCCTGATGCTTCAAAACCGGAAGACTGGGAT
GAGCGGGCCAAGATCGATGATCCCACAGACTCCAAGCCTGAGGACTGGGACAAGCCCGAG
CATATCCCTGACCCTGATGCTAAGAAGCCCGAGGACTGGGATGAAGAGATGGACGGAGAG
TGGGAACCCCCAGTGATTCAGAACCCTGAGTACAAGGGTGAGTGGAAGCCCCGGCAGATC
GACAACCCAGATTACAAGGGCACTTGGATCCACCCAGAAATTGACAACCCCGAGTATTCT
CCCGATCCCAGTATCTATGCCTATGATAACTTTGGCGTGCTGGGCCTGGACCTCTGGCAG
GTCAAGTCTGGCACCATCTTTGACAACTTCCTCATCACCAACGATGAGGCATACGCTGAG
GAGTTTGGCAACGAGACGTGGGGCGTAACAAAGGCAGCAGAGAAACAAATGAAGGACAAA
CAGGACGAGGAGCAGAGGCTTAAGGAGGAGGAAGAAGACAAGAAACGCAAAGAGGAGGAG
GAGGCAGAGGACAAGGAGGATGATGAGGACAAAGATGAGGATGAGGAGGATGAGGAGGAC
AAGGAGGAAGATGAGGAGGAAGATGTCCCCGGCCAGGCCAAGGACGAGCTGTAG
Target 9 GenBank Gene ID
Target 9 GeneCard ID CALR Link Image
Target 9 GenAtlas ID CALR Link Image
Target 9 HGNC ID HGNC:1455 Link Image
Target 9 Chromosome Location 19
Target 9 Locus 19p13.3-p13.2
Target 9 SNPs SNPJam Report Link Image
Target 9 General References
  1. Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed Link Image]
  2. McCauliffe DP, Yang YS, Wilson J, Sontheimer RD, Capra JD: The 5'-flanking region of the human calreticulin gene shares homology with the human GRP78, GRP94, and protein disulfide isomerase promoters. J Biol Chem. 1992 Feb 5;267(4):2557-62. [PubMed Link Image]
  3. Rojiani MV, Finlay BB, Gray V, Dedhar S: In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin alpha subunits. Biochemistry. 1991 Oct 15;30(41):9859-66. [PubMed Link Image]
  4. Rokeach LA, Haselby JA, Meilof JF, Smeenk RJ, Unnasch TR, Greene BM, Hoch SO: Characterization of the autoantigen calreticulin. J Immunol. 1991 Nov 1;147(9):3031-9. [PubMed Link Image]
  5. McCauliffe DP, Lux FA, Lieu TS, Sanz I, Hanke J, Newkirk MM, Bachinski LL, Itoh Y, Siciliano MJ, Reichlin M, et al.: Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen. J Clin Invest. 1990 May;85(5):1379-91. [PubMed Link Image]
  6. Krause KH, Simmerman HK, Jones LR, Campbell KP: Sequence similarity of calreticulin with a Ca2(+)-binding protein that co-purifies with an Ins(1,4,5)P3-sensitive Ca2+ store in HL-60 cells. Biochem J. 1990 Sep 1;270(2):545-8. [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]
  3. Srour MA, Grupp J, Aburubaiha Z, Albert T, Brondke H, Oldenburg J, Schwaab R: Modified expression of coagulation factor VIII by addition of a glycosylation site at the N terminus of the protein. Ann Hematol. 2007 Sep 26;. [PubMed Link Image]
  4. Pipe SW, Morris JA, Shah J, Kaufman RJ: Differential interaction of coagulation factor VIII and factor V with protein chaperones calnexin and calreticulin. J Biol Chem. 1998 Apr 3;273(14):8537-44. [PubMed Link Image]
  5. Kaufman RJ, Pipe SW, Tagliavacca L, Swaroop M, Moussalli M: Biosynthesis, assembly and secretion of coagulation factor VIII. Blood Coagul Fibrinolysis. 1997 Dec;8 Suppl 2:S3-14. [PubMed Link Image]
Drug Target 10 [top]
Target 10 ID 3831
Target 10 Name Low-density lipoprotein receptor-related protein 1
Target 10 Synonyms
  1. A2MR
  2. APOER
  3. Alpha-2-macroglobulin receptor
  4. Apolipoprotein E receptor
  5. CD91 antigen
  6. LRP
  7. Low-density lipoprotein receptor-related protein 1 precursor
Target 10 Gene Name LRP1
Target 10 Protein Sequence >Low-density lipoprotein receptor-related protein 1
MLTPPLLLLLPLLSALVAAAIDAPKTCSPKQFACRDQITCISKGWRCDGERDCPDGSDEA
PEICPQSKAQRCQPNEHNCLGTELCVPMSRLCNGVQDCMDGSDEGPHCRELQGNCSRLGC
QHHCVPTLDGPTCYCNSSFQLQADGKTCKDFDECSVYGTCSQLCTNTDGSFICGCVEGYL
LQPDNRSCKAKNEPVDRPPVLLIANSQNILATYLSGAQVSTITPTSTRQTTAMDFSYANE
TVCWVHVGDSAAQTQLKCARMPGLKGFVDEHTINISLSLHHVEQMAIDWLTGNFYFVDDI
DDRIFVCNRNGDTCVTLLDLELYNPKGIALDPAMGKVFFTDYGQIPKVERCDMDGQNRTK
LVDSKIVFPHGITLDLVSRLVYWADAYLDYIEVVDYEGKGRQTIIQGILIEHLYGLTVFE
NYLYATNSDNANAQQKTSVIRVNRFNSTEYQVVTRVDKGGALHIYHQRRQPRVRSHACEN
DQYGKPGGCSDICLLANSHKARTCRCRSGFSLGSDGKSCKKPEHELFLVYGKGRPGIIRG
MDMGAKVPDEHMIPIENLMNPRALDFHAETGFIYFADTTSYLIGRQKIDGTERETILKDG
IHNVEGVAVDWMGDNLYWTDDGPKKTISVARLEKAAQTRKTLIEGKMTHPRAIVVDPLNG
WMYWTDWEEDPKDSRRGRLERAWMDGSHRDIFVTSKTVLWPNGLSLDIPAGRLYWVDAFY
DRIETILLNGTDRKIVYEGPELNHAFGLCHHGNYLFWTEYRSGSVYRLERGVGGAPPTVT
LLRSERPPIFEIRMYDAQQQQVGTNKCRVNNGGCSSLCLATPGSRQCACAEDQVLDADGV
TCLANPSYVPPPQCQPGEFACANSRCIQERWKCDGDNDCLDNSDEAPALCHQHTCPSDRF
KCENNRCIPNRWLCDGDNDCGNSEDESNATCSARTCPPNQFSCASGRCIPISWTCDLDDD
CGDRSDESASCAYPTCFPLTQFTCNNGRCININWRCDNDNDCGDNSDEAGCSHSCSSTQF
KCNSGRCIPEHWTCDGDNDCGDYSDETHANCTNQATRPPGGCHTDEFQCRLDGLCIPLRW
RCDGDTDCMDSSDEKSCEGVTHVCDPSVKFGCKDSARCISKAWVCDGDNDCEDNSDEENC
ESLACRPPSHPCANNTSVCLPPDKLCDGNDDCGDGSDEGELCDQCSLNNGGCSHNCSVAP
GEGIVCSCPLGMELGPDNHTCQIQSYCAKHLKCSQKCDQNKFSVKCSCYEGWVLEPDGES
CRSLDPFKPFIIFSNRHEIRRIDLHKGDYSVLVPGLRNTIALDFHLSQSALYWTDVVEDK
IYRGKLLDNGALTSFEVVIQYGLATPEGLAVDWIAGNIYWVESNLDQIEVAKLDGTLRTT
LLAGDIEHPRAIALDPRDGILFWTDWDASLPRIEAASMSGAGRRTVHRETGSGGWPNGLT
VDYLEKRILWIDARSDAIYSARYDGSGHMEVLRGHEFLSHPFAVTLYGGEVYWTDWRTNT
LAKANKWTGHNVTVVQRTNTQPFDLQVYHPSRQPMAPNPCEANGGQGPCSHLCLINYNRT
VSCACPHLMKLHKDNTTCYEFKKFLLYARQMEIRGVDLDAPYYNYIISFTVPDIDNVTVL
DYDAREQRVYWSDVRTQAIKRAFINGTGVETVVSADLPNAHGLAVDWVSRNLFWTSYDTN
KKQINVARLDGSFKNAVVQGLEQPHGLVVHPLRGKLYWTDGDNISMANMDGSNRTLLFSG
QKGPVGLAIDFPESKLYWISSGNHTINRCNLDGSGLEVIDAMRSQLGKATALAIMGDKLW
WADQVSEKMGTCSKADGSGSVVLRNSTTLVMHMKVYDESIQLDHKGTNPCSVNNGDCSQL
CLPTSETTRSCMCTAGYSLRSGQQACEGVGSFLLYSVHEGIRGIPLDPNDKSDALVPVSG
TSLAVGIDFHAENDTIYWVDMGLSTISRAKRDQTWREDVVTNGIGRVEGIAVDWIAGNIY
WTDQGFDVIEVARLNGSFRYVVISQGLDKPRAITVHPEKGYLFWTEWGQYPRIERSRLDG
TERVVLVNVSISWPNGISVDYQDGKLYWCDARTDKIERIDLETGENREVVLSSNNMDMFS
VSVFEDFIYWSDRTHANGSIKRGSKDNATDSVPLRTGIGVQLKDIKVFNRDRQKGTNVCA
VANGGCQQLCLYRGRGQRACACAHGMLAEDGASCREYAGYLLYSERTILKSIHLSDERNL
NAPVQPFEDPEHMKNVIALAFDYRAGTSPGTPNRIFFSDIHFGNIQQINDDGSRRITIVE
NVGSVEGLAYHRGWDTLYWTSYTTSTITRHTVDQTRPGAFERETVITMSGDDHPRAFVLD
ECQNLMFWTNWNEQHPSIMRAALSGANVLTLIEKDIRTPNGLAIDHRAEKLYFSDATLDK
IERCEYDGSHRYVILKSEPVHPFGLAVYGEHIFWTDWVRRAVQRANKHVGSNMKLLRVDI
PQQPMGIIAVANDTNSCELSPCRINNGGCQDLCLLTHQGHVNCSCRGGRILQDDLTCRAV
NSSCRAQDEFECANGECINFSLTCDGVPHCKDKSDEKPSYCNSRRCKKTFRQCSNGRCVS
NMLWCNGADDCGDGSDEIPCNKTACGVGEFRCRDGTCIGNSSRCNQFVDCEDASDEMNCS
ATDCSSYFRLGVKGVLFQPCERTSLCYAPSWVCDGANDCGDYSDERDCPGVKRPRCPLNY
FACPSGRCIPMSWTCDKEDDCEHGEDETHCNKFCSEAQFECQNHRCISKQWLCDGSDDCG
DGSDEAAHCEGKTCGPSSFSCPGTHVCVPERWLCDGDKDCADGADESIAAGCLYNSTCDD
REFMCQNRQCIPKHFVCDHDRDCADGSDESPECEYPTCGPSEFRCANGRCLSSRQWECDG
ENDCHDQSDEAPKNPHCTSPEHKCNASSQFLCSSGRCVAEALLCNGQDDCGDSSDERGCH
INECLSRKLSGCSQDCEDLKIGFKCRCRPGFRLKDDGRTCADVDECSTTFPCSQRCINTH
GSYKCLCVEGYAPRGGDPHSCKAVTDEEPFLIFANRYYLRKLNLDGSNYTLLKQGLNNAV
ALDFDYREQMIYWTDVTTQGSMIRRMHLNGSNVQVLHRTGLSNPDGLAVDWVGGNLYWCD
KGRDTIEVSKLNGAYRTVLVSSGLREPRALVVDVQNGYLYWTDWGDHSLIGRIGMDGSSR
SVIVDTKITWPNGLTLDYVTERIYWADAREDYIEFASLDGSNRHVVLSQDIPHIFALTLF
EDYVYWTDWETKSINRAHKTTGTNKTLLISTLHRPMDLHVFHALRQPDVPNHPCKVNNGG
CSNLCLLSPGGGHKCACPTNFYLGSDGRTCVSNCTASQFVCKNDKCIPFWWKCDTEDDCG
DHSDEPPDCPEFKCRPGQFQCSTGICTNPAFICDGDNDCQDNSDEANCDIHVCLPSQFKC
TNTNRCIPGIFRCNGQDNCGDGEDERDCPEVTCAPNQFQCSITKRCIPRVWVCDRDNDCV
DGSDEPANCTQMTCGVDEFRCKDSGRCIPARWKCDGEDDCGDGSDEPKEECDERTCEPYQ
FRCKNNRCVPGRWQCDYDNDCGDNSDEESCTPRPCSESEFSCANGRCIAGRWKCDGDHDC
ADGSDEKDCTPRCDMDQFQCKSGHCIPLRWRCDADADCMDGSDEEACGTGVRTCPLDEFQ
CNNTLCKPLAWKCDGEDDCGDNSDENPEECARFVCPPNRPFRCKNDRVCLWIGRQCDGTD
NCGDGTDEEDCEPPTAHTTHCKDKKEFLCRNQRCLSSSLRCNMFDDCGDGSDEEDCSIDP
KLTSCATNASICGDEARCVRTEKAAYCACRSGFHTVPGQPGCQDINECLRFGTCSQLCNN
TKGGHLCSCARNFMKTHNTCKAEGSEYQVLYIADDNEIRSLFPGHPHSAYEQAFQGDESV
RIDAMDVHVKAGRVYWTNWHTGTISYRSLPPAAPPTTSNRHRRQIDRGVTHLNISGLKMP
RGIAIDWVAGNVYWTDSGRDVIEVAQMKGENRKTLISGMIDEPHAIVVDPLRGTMYWSDW
GNHPKIETAAMDGTLRETLVQDNIQWPTGLAVDYHNERLYWADAKLSVIGSIRLNGTDPI
VAADSKRGLSHPFSIDVFEDYIYGVTYINNRVFKIHKFGHSPLVNLTGGLSHASDVVLYH
QHKQPEVTNPCDRKKCEWLCLLSPSGPVCTCPNGKRLDNGTCVPVPSPTPPPDAPRPGTC
NLQCFNGGSCFLNARRQPKCRCQPRYTGDKCELDQCWEHCRNGGTCAASPSGMPTCRCPT
GFTGPKCTQQVCAGYCANNSTCTVNQGNQPQCRCLPGFLGDRCQYRQCSGYCENFGTCQM
AADGSRQCRCTAYFEGSRCEVNKCSRCLEGACVVNKQSGDVTCNCTDGRVAPSCLTCVGH
CSNGGSCTMNSKMMPECQCPPHMTGPRCEEHVFSQQQPGHIASILIPLLLLLLLVLVAGV
VFWYKRRVQGAKGFQHQRMTNGAMNVEIGNPTYKMYEGGEPDDVGGLLDADFALDPDKPT
NFTNPVYATLYMGGHGSRHSLASTDEKRELLGRGPEDEIGDPLA
Target 10 Number of Residues 4619
Target 10 Molecular Weight 504578
Target 10 Theoretical pI 5.02
Target 10 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
cell
membrane
Target 10 General Function Not Available
Target 10 Specific Function Required for early embryonic development. Involved in the plasma clearance of chylomicron remnants and activated alpha 2-macroglobulin, as well as the local metabolism of complexes between plasminogen activators and their endogenous inhibitors. May modulate APP metabolism, kinase-dependent intracellular signaling, neuronal calcium signaling as well as neurotransmission
Target 10 Pathways Not Available
Target 10 Reactions Not Available
Target 10 Pfam Domain Function
Target 10 Signals
  • 1-19
Target 10 Transmembrane Regions
  • 4420-4444
Target 10 Essentiality Non-Essential
Target 10 GenBank ID Protein 34339 Link Image
Target 10 UniProtKB/Swiss-Prot ID Q07954 Link Image
Target 10 UniProtKB/Swiss-Prot Entry Name LRP1_HUMAN Link Image
Target 10 PDB ID Not Available
Target 10 Cellular Location
  • Cell membrane
Target 10 Gene Sequence >13635 bp
ATGCTGACCCCGCCGTTGCTCCTGCTGCTGCCCCTGCTCTCAGCTCTGGTCGCGGCGGCT
ATCGACGCCCCTAAGACTTGCAGCCCCAAGCAGTTTGCCTGCAGAGATCAAATAACCTGT
ATCTCAAAGGGCTGGCGGTGCGACGGTGAGAGGGACTGCCCAGACGGATCTGACGAGGCC
CCTGAGATTTGTCCACAGAGTAAGGCCCAGCGATGCCAGCCAAACGAGCATAACTGCCTG
GGTACTGAGCTGTGTGTTCCCATGTCCCGCCTCTGCAATGGGGTCCAGGACTGCATGGAC
GGCTCAGATGAGGGGCCCCACTGCCGAGAGCTCCAAGGCAACTGCTCTCGCCTGGGCTGC
CAGCACCATTGTGTCCCCACACTCGATGGGCCCACCTGCTACTGCAACAGCAGCTTTCAG
CTTCAGGCAGATGGCAAGACCTGCAAAGATTTTGATGAGTGCTCAGTGTACGGCACCTGC
AGCCAGCTATGCACCAACACAGACGGCTCCTTCATATGTGGCTGTGTTGAAGGATACCTC
CTGCAGCCGGATAACCGCTCCTGCAAGGCCAAGAACGAGCCAGTAGACCGGCCCCCTGTG
CTGTTGATAGCCAACTCCCAGAACATCTTGGCCACGTACCTGAGTGGGGCCCAGGTGTCT
ACCATCACACCTACGAGCACGCGGCAGACCACAGCCATGGACTTCAGCTATGCCAACGAG
ACCGTATGCTGGGTGCATGTTGGGGACAGTGCTGCTCAGACGCAGCTCAAGTGTGCCCGC
ATGCCTGGCCTAAAGGGCTTCGTGGATGAGCACACCATCAACATCTCCCTCAGTCTGCAC
CACGTGGAACAGATGGCCATCGACTGGCTGACAGGCAACTTCTACTTTGTGGATGACATC
GATGATAGGATCTTTGTCTGCAACAGAAATGGGGACACATGTGTCACATTGCTAGACCTG
GAACTCTACAACCCCAAGGGCATTGCCCTGGACCCTGCCATGGGGAAGGTGTTTTTCACT
GACTATGGGCAGATCCCAAAGGTGGAACGCTGTGACATGGATGGGCAGAACCGCACCAAG
CTCGTCGACAGCAAGATTGTGTTTCCTCATGGCATCACGCTGGACCTGGTCAGCCGCCTT
GTCTACTGGGCAGATGCCTATCTGGACTATATTGAAGTGGTGGACTATGAGGGCAAGGGC
CGCCAGACCATCATCCAGGGCATCCTGATTGAGCACCTGTACGGCCTGACTGTGTTTGAG
AATTATCTCTATGCCACCAACTCGGACAATGCCAATGCCCAGCAGAAGACGAGTGTGATC
CGTGTGAACCGCTTTAACAGCACCGAGTACCAGGTTGTCACCCGGGTGGACAAGGGTGGT
GCCCTCCACATCTACCACCAGAGGCGTCAGCCCCGAGTGAGGAGCCATGCCTGTGAAAAC
GACCAGTATGGGAAGCCGGGTGGCTGCTCTGACATCTGCCTGCTGGCCAACAGCCACAAG
GCGCGGACCTGCCGCTGCCGTTCCGGCTTCAGCCTGGGCAGTGACGGGAAGTCATGCAAG
AAGCCGGAGCATGAGCTGTTCCTCGTGTATGGCAAGGGCCGGCCAGGCATCATCCGGGGC
ATGGATATGGGGGCCAAGGTCCCGGATGAGCACATGATCCCCATTGAAAACCTCATGAAC
CCCCGAGCCCTGGACTTCCACGCTGAGACCGGCTTCATCTACTTTGCCGACACCACCAGC
TACCTCATTGGCCGCCAGAAGATTGATGGCACTGAGCGGGAGACCATCCTGAAGGACGGC
ATCCACAATGTGGAGGGTGTGGCCGTGGACTGGATGGGAGACAATCTGTACTGGACGGAC
GATGGGCCCAAAAAGACAATCAGCGTGGCCAGGCTGGAGAAAGCTGCTCAGACCCGCAAG
ACTTTAATCGAGGGCAAAATGACACACCCCAGGGCTATTGTGGTGGATCCACTCAATGGG
TGGATGTACTGGACAGACTGGGAGGAGGACCCCAAGGACAGTCGGCGTGGGCGGCTGGAG
AGGGCGTGGATGGATGGCTCACACCGAGACATCTTTGTCACCTCCAAGACAGTGCTTTGG
CCCAATGGGCTAAGCCTGGACATCCCGGCTGGGCGCCTCTACTGGGTGGATGCCTTCTAC
GACCGCATCGAGACGATACTGCTCAATGGCACAGACCGGAAGATTGTGTATGAAGGTCCT
GAGCTGAACCACGCCTTTGGCCTGTGTCACCATGGCAACTACCTCTTCTGGACTGAGTAT
CGGAGTGGCAGTGTCTACCGCTTGGAACGGGGTGTAGGAGGCGCACCCCCCACTGTGACC
CTTCTGCGCAGTGAGCGGCCCCCCATCTTTGAGATCCGAATGTATGATGCCCAGCAGCAG
CAAGTTGGCACCAACAAATGCCGGGTGAACAATGGCGGCTGCAGCAGCCTGTGCTTGGCC
ACCCCTGGGAGCCGCCAGTGCGCCTGTGCTGAGGACCAGGTGTTGGACGCAGACGGCGTC
ACTTGCTTGGCGAACCCATCCTACGTGCCTCCACCCCAGTGCCAGCCAGGCGAGTTTGCC
TGTGCCAACAGCCGCTGCATCCAGGAGCGCTGGAAGTGTGACGGAGACAACGATTGCCTG
GACAACAGTGATGAGGCCCCAGCCCTCTGCCATCAGCACACCTGCCCCTCGGACCGATTC
AAGTGCGAGAACAACCGGTGCATCCCCAACCGCTGGCTCTGCGACGGGGACAATGACTGT
GGGAACAGTGAAGATGAGTCCAATGCCACTTGTTCAGCCCGCACCTGCCCCCCCAACCAG
TTCTCCTGTGCCAGTGGCCGCTGCATCCCCATCTCCTGGACGTGTGATCTGGATGACGAC
TGTGGGGACCGCTCTGATGAGTCTGCTTCGTGTGCCTATCCCACCTGCTTCCCCCTGACT
CAGTTTACCTGCAACAATGGCAGATGTATCAACATCAACTGGAGATGCGACAATGACAAT
GACTGTGGGGACAACAGTGACGAAGCCGGCTGCAGCCACTCCTGTTCTAGCACCCAGTTC
AAGTGCAACAGCGGGCGTTGCATCCCCGAGCACTGGACCTGCGATGGGGACAATGACTGC
GGAGACTACAGTGATGAGACACACGCCAACTGCACCAACCAGGCCACGAGGCCCCCTGGT
GGCTGCCACACTGATGAGTTCCAGTGCCGGCTGGATGGACTATGCATCCCCCTGCGGTGG
CGCTGCGATGGGGACACTGACTGCATGGACTCCAGCGATGAGAAGAGCTGTGAGGGAGTG
ACCCACGTCTGCGATCCCAGTGTCAAGTTTGGCTGCAAGGACTCAGCTCGGTGCATCAGC
AAAGCGTGGGTGTGTGATGGCGACAATGACTGTGAGGATAACTCGGACGAGGAGAACTGC
GAGTCCCTGGCCTGCAGGCCACCCTCGCACCCTTGTGCCAACAACACCTCAGTCTGCCTG
CCCCCTGACAAGCTGTGTGATGGCAACGACGACTGTGGCGACGGCTCAGATGAGGGCGAG
CTCTGCGACCAGTGCTCTCTGAATAACGGTGGCTGCAGCCACAACTGCTCAGTGGCACCT
GGCGAAGGCATTGTGTGTTCCTGCCCTCTGGGCATGGAGCTGGGGCCCGACAACCACACC
TGCCAGATCCAGAGCTACTGTGCCAAGCATCTCAAATGCAGCCAAAAGTGCGACCAGAAC
AAGTTCAGCGTGAAGTGCTCCTGCTACGAGGGCTGGGTCCTGGAACCTGACGGCGAGAGC
TGCCGCAGCCTGGACCCCTTCAAGCCGTTCATCATTTTCTCCAACCGCCATGAAATCCGG
CGCATCGATCTTCACAAAGGAGACTACAGCGTCCTGGTGCCCGGCCTGCGCAACACCATC
GCCCTGGACTTCCACCTCAGCCAGAGCGCCCTCTACTGGACCGACGTGGTGGAGGACAAG
ATCTACCGCGGGAAGCTGCTGGACAACGGAGCCCTGACTAGTTTCGAGGTGGTGATTCAG
TATGGCCTGGCCACACCCGAGGGCCTGGCTGTAGACTGGATTGCAGGCAACATCTACTGG
GTGGAGAGTAACCTGGATCAGATCGAGGTGGCCAAGCTGGATGGGACCCTCCGGACCACC
CTGCTGGCCGGTGACATTGAGCACCCAAGGGCAATCGCACTGGATCCCCGGGATGGGATC
CTGTTTTGGACAGACTGGGATGCCAGCCTGCCCCGCATTGAGGCAGCCTCCATGAGTGGG
GCTGGGCGCCGCACCGTGCACCGGGAGACCGGCTCTGGGGGCTGGCCCAACGGGCTCACC
GTGGACTACCTGGAGAAGCGCATCCTTTGGATTGACGCCAGGTCAGATGCCATTTACTCA
GCCCGTTACGACGGCTCTGGCCACATGGAGGTGCTTCGGGGACACGAGTTCCTGTCGCAC
CCGTTTGCAGTGACGCTGTACGGGGGGGAGGTCTACTGGACTGACTGGCGAACAAACACA
CTGGCTAAGGCCAACAAGTGGACCGGCCACAATGTCACCGTGGTACAGAGGACCAACACC
CAGCCCTTTGACCTGCAGGTGTACCACCCCTCCCGCCAGCCCATGGCTCCCAATCCCTGT
GAGGCCAATGGGGGCCAGGGCCCCTGCTCCCACCTGTGTCTCATCAACTACAACCGGACC
GTGTCCTGCGCCTGCCCCCACCTCATGAAGCTCCACAAGGACAACACCACCTGCTATGAG
TTTAAGAAGTTCCTGCTGTACGCACGTCAGATGGAGATCCGAGGTGTGGACCTGGATGCT
CCCTACTACAACTACATCATCTCCTTCACGGTGCCCGACATCGACAACGTCACAGTGCTA
GACTACGATGCCCGCGAGCAGCGTGTGTACTGGTCTGACGTGCGGACACAGGCCATCAAG
CGGGCCTTCATCAACGGCACAGGCGTGGAGACAGTCGTCTCTGCAGACTTGCCAAATGCC
CACGGGCTGGCTGTGGACTGGGTCTCCCGAAACCTGTTCTGGACAAGCTATGACACCAAT
AAGAAGCAGATCAATGTGGCCCGGCTGGATGGCTCCTTCAAGAACGCAGTGGTGCAGGGC
CTGGAGCAGCCCCATGGCCTTGTCGTCCACCCTCTGCGTGGGAAGCTCTACTGGACCGAT
GGTGACAACATCAGCATGGCCAACATGGATGGCAGCAATCGCACCCTGCTCTTCAGTGGC
CAGAAGGGCCCCGTGGGCCTGGCTATTGACTTCCCTGAAAGCAAACTCTACTGGATCAGC
TCCGGGAACCATACCATCAACCGCTGCAACCTGGATGGGAGTGGGCTGGAGGTCATCGAT
GCCATGCGGAGCCAGCTGGGCAAGGCCACCGCCCTGGCCATCATGGGGGACAAGCTGTGG
TGGGCTGATCAGGTGTCGGAAAAGATGGGCACATGCAGCAAGGCTGACGGCTCGGGCTCC
GTGGTCCTTCGGAACAGCACCACCCTGGTGATGCACATGAAGGTCTATGACGAGAGCATC
CAGCTGGACCATAAGGGCACCAACCCCTGCAGTGTCAACAACGGTGACTGCTCCCAGCTC
TGCCTGCCCACGTCAGAGACGACCCGCTCCTGCATGTGCACAGCCGGCTATAGCCTCCGG
AGTGGCCAGCAGGCCTGCGAGGGCGTAGGTTCCTTTCTCCTGTACTCTGTGCATGAGGGA
ATCAGGGGAATTCCCCTGGATCCCAATGACAAGTCAGATGCCCTGGTCCCAGTGTCCGGG
ACCTCGCTGGCTGTCGGCATCGACTTCCACGCTGAAAATGACACCATCTACTGGGTGGAC
ATGGGCCTGAGCACGATCAGCCGGGCCAAGCGGGACCAGACGTGGCGTGAAGACGTGGTG
ACCAATGGCATTGGCCGTGTGGAGGGCATTGCAGTGGACTGGATCGCAGGCAACATCTAC
TGGACAGACCAGGGCTTTGATGTCATCGAGGTCGCCCGGCTCAATGGCTCCTTCCGCTAC
GTGGTGATCTCCCAGGGTCTAGACAAGCCCCGGGCCATCACCGTCCACCCGGAGAAAGGG
TACTTGTTCTGGACTGAGTGGGGTCAGTATCCGCGTATTGAGCGGTCTCGGCTAGATGGC
ACGGAGCGTGTGGTGCTGGTCAACGTCAGCATCAGCTGGCCCAACGGCATCTCAGTGGAC
TACCAGGATGGGAAGCTGTACTGGTGCGATGCACGGACAGACAAGATTGAACGGATCGAC
CTGGAGACAGGTGAGAACCGCGAGGTGGTTCTGTCCAGCAACAACATGGACATGTTTTCA
GTGTCTGTGTTTGAGGATTTCATCTACTGGAGTGACAGGACTCATGCCAACGGCTCTATC
AAGCGCGGGAGCAAAGACAATGCCACAGACTCCGTGCCCCTGCGAACCGGCATCGGCGTC
CAGCTTAAAGACATCAAAGTCTTCAACCGGGACCGGCAGAAAGGCACCAACGTGTGCGCG
GTGGCCAATGGCGGGTGCCAGCAGCTGTGCCTGTACCGGGGCCGTGGGCAGCGGGCCTGC
GCCTGTGCCCACGGGATGCTGGCTGAAGACGGAGCATCGTGCCGCGAGTATGCCGGCTAC
CTGCTCTACTCAGAGCGCACCATTCTCAAGAGTATCCACCTGTCGGATGAGCGCAACCTC
AATGCGCCCGTGCAGCCCTTCGAGGACCCTGAGCACATGAAGAACGTCATCGCCCTGGCC
TTTGACTACCGGGCAGGCACCTCTCCGGGCACCCCCAATCGCATCTTCTTCAGCGACATC
CACTTTGGGAACATCCAACAGATCAACGACGATGGCTCCAGGAGGATCACCATTGTGGAA
AACGTGGGCTCCGTGGAAGGCCTGGCCTATCACCGTGGCTGGGACACTCTCTATTGGACA
AGCTACACGACATCCACCATCACGCGCCACACAGTGGACCAGACCCGCCCAGGGGCCTTC
GAGCGTGAGACCGTCATCACTATGTCTGGAGATGACCACCCACGGGCCTTCGTTTTGGAC
GAGTGCCAGAACCTCATGTTCTGGACCAACTGGAATGAGCAGCATCCCAGCATCATGCGG
GCGGCGCTCTCGGGAGCCAATGTCCTGACCCTTATCGAGAAGGACATCCGTACCCCCAAT
GGCCTGGCCATCGACCACCGTGCCGAGAAGCTCTACTTCTCTGACGCCACCCTGGACAAG
ATCGAGCGGTGCGAGTATGACGGCTCCCACCGCTATGTGATCCTAAAGTCAGAGCCTGTC
CACCCCTTCGGGCTGGCCGTGTATGGGGAGCACATTTTCTGGACTGACTGGGTGCGGCGG
GCAGTGCAGCGGGCCAACAAGCACGTGGGCAGCAACATGAAGCTGCTGCGCGTGGACATC
CCCCAGCAGCCCATGGGCATCATCGCCGTGGCCAACGACACCAACAGCTGTGAACTCTCT
CCATGCCGAATCAACAACGGTGGCTGCCAGGACCTGTGTCTGCTCACTCACCAGGGCCAT
GTCAACTGCTCATGCCGAGGGGGCCGAATCCTCCAGGATGACCTCACCTGCCGAGCGGTG
AATTCCTCTTGCCGAGCACAAGATGAGTTTGAGTGTGCCAATGGCGAGTGCATCAACTTC
AGCCTGACCTGCGACGGCGTCCCCCACTGCAAGGACAAGTCCGATGAGAAGCCATCCTAC
TGCAACTCCCGCCGCTGCAAGAAGACTTTCCGGCAGTGCAGCAATGGGCGCTGTGTGTCC
AACATGCTGTGGTGCAACGGGGCCGACGACTGTGGGGATGGCTCTGACGAGATCCCTTGC
AACAAGACAGCCTGTGGTGTGGGCGAGTTCCGCTGCCGGGACGGGACCTGCATCGGGAAC
TCCAGCCGCTGCAACCAGTTTGTGGATTGTGAGGACGCCTCAGATGAGATGAACTGCAGT
GCCACCGACTGCAGCAGCTACTTCCGCCTGGGCGTGAAGGGCGTGCTCTTCCAGCCCTGC
GAGCGGACCTCACTCTGCTACGCACCCAGCTGGGTGTGTGATGGCGCCAATGACTGTGGG
GACTACAGTGATGAGCGCGACTGCCCAGGTGTGAAACGCCCCAGATGCCCTCTGAATTAC
TTCGCCTGCCCTAGTGGGCGCTGCATCCCCATGAGCTGGACGTGTGACAAAGAGGATGAC
TGTGAACATGGCGAGGACGAGACCCACTGCAACAAGTTCTGCTCAGAGGCCCAGTTTGAG
TGCCAGAACCATCGCTGCATCTCCAAGCAGTGGCTGTGTGACGGCAGCGATGACTGTGGG
GATGGCTCAGACGAGGCTGCTCACTGTGAAGGCAAGACGTGCGGCCCCTCCTCCTTCTCC
TGCCCTGGCACCCACGTGTGCGTCCCCGAGCGCTGGCTCTGTGACGGTGACAAAGACTGT
GCTGATGGTGCAGACGAGAGCATCGCAGCTGGTTGCTTGTACAACAGCACTTGTGACGAC
CGTGAGTTCATGTGCCAGAACCGCCAGTGCATCCCCAAGCACTTCGTGTGTGACCACGAC
CGTGACTGTGCAGATGGCTCTGATGAGTCCCCCGAGTGTGAGTACCCGACCTGCGGCCCC
AGTGAGTTCCGCTGTGCCAATGGGCGCTGTCTGAGCTCCCGCCAGTGGGAGTGTGATGGC
GAGAATGACTGCCACGACCAGAGTGACGAGGCTCCCAAGAACCCACACTGCACCAGCCCA
GAGCACAAGTGCAATGCCTCGTCACAGTTCCTGTGCAGCAGTGGGCGCTGTGTGGCTGAG
GCACTGCTCTGCAACGGCCAGGATGACTGTGGCGACAGCTCGGACGAGCGTGGCTGCCAC
ATCAATGAGTGTCTCAGCCGCAAGCTCAGTGGCTGCAGCCAGGACTGTGAGGACCTCAAG
ATCGGCTTCAAGTGCCGCTGTCGCCCTGGCTTCCGGCTGAAGGATGACGGCCGGACGTGT
GCTGATGTGGACGAGTGCAGCACCACCTTCCCCTGCAGCCAGCGCTGCATCAACACCCAT
GGCAGCTATAAGTGTCTGTGTGTGGAGGGCTATGCACCCCGCGGCGGCGACCCCCACAGC
TGCAAGGCTGTGACTGACGAGGAACCGTTTCTGATCTTCGCCAACCGGTACTACCTGCGC
AAGCTCAACCTGGACGGGTCCAACTACACGTTACTTAAGCAGGGCCTGAACAACGCCGTT
GCCTTGGATTTTGACTACCGAGAGCAGATGATCTACTGGACAGATGTGACCACCCAGGGC
AGCATGATCCGAAGGATGCACCTTAACGGGAGCAATGTGCAGGTCCTACACCGTACAGGC
CTCAGCAACCCCGATGGGCTGGCTGTGGACTGGGTGGGTGGCAACCTGTACTGGTGCGAC
AAAGGCCGGGACACCATCGAGGTGTCCAAGCTCAATGGGGCCTATCGGACGGTGCTGGTC
AGCTCTGGCCTCCGTGAGCCCAGGGCTCTGGTGGTGGATGTGCAGAATGGGTACCTGTAC
TGGACAGACTGGGGTGACCATTCACTGATCGGCCGCATCGGCATGGATGGGTCCAGCCGC
AGCGTCATCGTGGACACCAAGATCACATGGCCCAATGGCCTGACGCTGGACTATGTCACT
GAGCGCATCTACTGGGCCGACGCCCGCGAGGACTACATTGAATTTGCCAGCCTGGATGGC
TCCAATCGCCACGTTGTGCTGAGCCAGGACATCCCGCACATCTTTGCACTGACCCTGTTT
GAGGACTACGTCTACTGGACCGACTGGGAAACAAAGTCCATTAACCGAGCCCACAAGACC
ACGGGCACCAACAAAACGCTCCTCATCAGCACGCTGCACCGGCCCATGGACCTGCATGTC
TTCCATGCCCTGCGCCAGCCAGACGTGCCCAATCACCCCTGCAAGGTCAACAATGGTGGC
TGCAGCAACCTGTGCCTGCTGTCCCCCGGGGGAGGGCACAAATGTGCCTGCCCCACCAAC
TTCTACCTGGGCAGCGATGGGCGCACCTGTGTGTCCAACTGCACGGCTAGCCAGTTTGTA
TGCAAGAACGACAAGTGCATCCCCTTCTGGTGGAAGTGTGACACCGAGGACGACTGCGGG
GACCACTCAGACGAGCCCCCGGACTGCCCTGAGTTCAAGTGCCGGCCCGGACAGTTCCAG
TGCTCCACAGGTATCTGCACAAACCCTGCCTTCATCTGCGATGGCGACAATGACTGCCAG
GACAACAGTGACGAGGCCAACTGTGACATCCACGTCTGCTTGCCCAGTCAGTTCAAATGC
ACCAACACCAACCGCTGTATTCCCGGCATCTTCCGCTGCAATGGGCAGGACAACTGCGGA
GATGGGGAGGATGAGAGGGACTGCCCCGAGGTGACCTGCGCCCCCAACCAGTTCCAGTGC
TCCATTACCAAACGGTGCATCCCCCGGGTCTGGGTCTGCGACCGGGACAATGACTGTGTG
GATGGCAGTGATGAGCCCGCCAACTGCACCCAGATGACCTGTGGTGTGGACGAGTTCCGC
TGCAAGGATTCGGGCCGCTGCATCCCAGCGCGTTGGAAGTGTGACGGAGAGGATGACTGT
GGGGATGGCTCGGATGAGCCCAAGGAAGAGTGTGATGAACGCACCTGTGAGCCATACCAG
TTCCGCTGCAAGAACAACCGCTGCGTGCCCGGCCGCTGGCAGTGCGACTACGACAACGAT
TGCGGTGACAACTCCGATGAAGAGAGCTGCACCCCTCGGCCCTGCTCCGAGAGTGAGTTC
TCCTGTGCCAACGGCCGCTGCATCGCGGGGCGCTGGAAATGCGATGGAGACCACGACTGC
GCGGACGGCTCGGACGAGAAAGACTGCACCCCCCGCTGTGACATGGACCAGTTCCAGTGC
AAGAGCGGCCACTGCATCCCCCTGCGCTGGCGCTGTGACGCAGACGCCGACTGCATGGAC
GGCAGCGACGAGGAGGCCTGCGGCACTGGCGTGCGGACCTGCCCCCTGGACGAGTTCCAG
TGCAACAACACCTTGTGCAAGCCGCTGGCCTGGAAGTGCGATGGCGAGGATGACTGTGGG
GACAACTCAGATGAGAACCCCGAGGAGTGTGCCCGGTTCGTGTGCCCTCCCAACCGGCCC
TTCCGTTGCAAGAATGACCGCGTCTGTCTGTGGATCGGGCGCCAATGCGATGGCACGGAC
AACTGTGGGGATGGGACTGATGAAGAGGACTGTGAGCCCCCCACAGCCCACACCACCCAC
TGCAAAGACAAGAAGGAGTTTCTGTGCCGGAACCAGCGCTGCCTCTCCTCCTCCCTGCGC
TGCAACATGTTCGATGACTGCGGGGACGGCTCTGACGAGGAGGACTGCAGCATCGACCCC
AAGCTGACCAGCTGCGCCACCAATGCCAGCATCTGTGGGGACGAGGCACGCTGCGTGCGC
ACCGAGAAAGCGGCCTACTGTGCCTGCCGCTCGGGCTTCCACACCGTGCCCGGCCAGCCC
GGATGCCAAGACATCAACGAGTGCCTGCGCTTCGGCACCTGCTCCCAGCTCTGCAACAAC
ACCAAGGGCGGCCACCTCTGCAGCTGCGCTCGGAACTTCATGAAGACGCACAACACCTGC
AAGGCCGAAGGCTCTGAGTACCAGGTCCTGTACATCGCTGATGACAATGAGATCCGCAGC
CTGTTCCCCGGCCACCCCCATTCGGCTTACGAGCAGGCATTCCAGGGTGACGAGAGTGTC
CGCATTGATGCTATGGATGTCCATGTCAAGGCTGGCCGTGTCTATTGGACCAACTGGCAC
ACGGGCACCATCTCCTACCGCAGCCTGCCACCTGCTGCGCCTCCTACCACTTCCAACCGC
CACCGGCGACAGATTGACCGGGGTGTCACCCACCTCAACATTTCAGGGCTGAAGATGCCC
AGAGGCATCGCCATCGACTGGGTGGCCGGAAACGTGTACTGGACCGACTCGGGCCGAGAT
GTGATTGAGGTGGCGCAGATGAAGGGCGAGAACCGCAAGACGCTCATCTCGGGCATGATT
GACGAGCCCCACGCCATTGTGGTGGACCCACTGAGGGGGACCATGTACTGGTCAGACTGG
GGCAACCACCCCAAGATTGAGACGGCAGCGATGGATGGGACGCTTCGGGAGACACTGGTG
CAGGACAACATTCAGTGGCCCACAGGCCTGGCCGTGGATTATCACAATGAGCGGCTGTAC
TGGGCAGACGCCAAGCTTTCAGTCATCGGCAGCATCCGGCTCAATGGCACGGACCCCATT
GTGGCTGCTGACAGCAAACGAGGCCTAAGTCACCCCTTCAGCATCGACGTCTTTGAGGAT
TACATCTATGGTGTCACCTACATCAATAATCGTGTCTTCAAGATCCATAAGTTTGGCCAC
AGCCCCTTGGTCAACCTGACAGGGGGCCTGAGCCACGCCTCTGACGTGGTCCTTTACCAT
CAGCACAAGCAGCCCGAAGTGACCAACCCATGTGACCGCAAGAAATGCGAGTGGCTCTGC
CTGCTGAGCCCCAGTGGGCCTGTCTGCACCTGTCCCAATGGGAAGCGGCTGGACAACGGC
ACATGCGTGCCTGTGCCCTCTCCAACGCCCCCCCCAGATGCTCCCCGGCCTGGAACCTGT
AACCTGCAGTGCTTCAACGGTGGCAGCTGTTTCCTCAATGCACGGAGGCAGCCCAAGTGC
CGCTGCCAACCCCGCTACACGGGTGACAAGTGTGAACTGGACCAGTGCTGGGAGCACTGT
CGCAATGGGGGCACCTGTGCTGCCTCCCCCTCTGGCATGCCCACGTGCCGGTGCCCCACG
GGCTTCACGGGCCCCAAATGCACCCAGCAGGTGTGTGCGGGCTACTGTGCCAACAACAGC
ACCTGCACTGTCAACCAGGGCAACCAGCCCCAGTGCCGATGCCTACCCGGCTTCCTGGGC
GACCGCTGCCAGTACCGGCAGTGCTCTGGCTACTGTGAGAACTTTGGCACATGCCAGATG
GCTGCTGATGGCTCCCGACAATGCCGCTGCACTGCCTACTTTGAGGGATCGAGGTGTGAG
GTGAACAAGTGCAGCCGCTGTCTCGAAGGGGCCTGTGTGGTCAACAAGCAGAGTGGGGAT
GTCACCTGCAACTGCACGGATGGCCGGGTGGCCCCCAGCTGTCTGACCTGCGTCGGCCAC
TGCAGCAATGGCGGCTCCTGTACCATGAACAGCAAAATGATGCCTGAGTGCCAGTGCCCA
CCCCACATGACAGGGCCCCGGTGTGAGGAGCACGTCTTCAGCCAGCAGCAGCCAGGACAT
ATAGCCTCCATCCTAATCCCTCTGCTGTTGCTGCTGCTGCTGGTTCTGGTGGCCGGAGTG
GTATTCTGGTATAAGCGGCGAGTCCAAGGGGCTAAGGGCTTCCAGCACCAACGGATGACC
AACGGGGCCATGAACGTGGAGATTGGAAACCCCACCTACAAGATGTACGAAGGCGGAGAG
CCTGATGATGTGGGAGGCCTACTGGACGCTGACTTTGCCCTGGACCCTGACAAGCCCACC
AACTTCACCAACCCCGTGTATGCCACACTCTACATGGGGGGCCATGGCAGTCGCCACTCC
CTGGCCAGCACGGACGAGAAGCGAGAACTCCTGGGCCGGGGCCCTGAGGACGAGATAGGG
GACCCCTTGGCATAG
Target 10 GenBank Gene ID
Target 10 GeneCard ID LRP1 Link Image
Target 10 GenAtlas ID LRP1 Link Image
Target 10 HGNC ID HGNC:6692 Link Image
Target 10 Chromosome Location 12
Target 10 Locus 12q13-q14
Target 10 SNPs SNPJam Report Link Image
Target 10 General References
  1. Kristensen T, Moestrup SK, Gliemann J, Bendtsen L, Sand O, Sottrup-Jensen L: Evidence that the newly cloned low-density-lipoprotein receptor related protein (LRP) is the alpha 2-macroglobulin receptor. FEBS Lett. 1990 Dec 10;276(1-2):151-5. [PubMed Link Image]
  2. Herz J, Kowal RC, Goldstein JL, Brown MS: Proteolytic processing of the 600 kd low density lipoprotein receptor-related protein (LRP) occurs in a trans-Golgi compartment. EMBO J. 1990 Jun;9(6):1769-76. [PubMed Link Image]
  3. Kutt H, Herz J, Stanley KK: Structure of the low-density lipoprotein receptor-related protein (LRP) promoter. Biochim Biophys Acta. 1989 Dec 22;1009(3):229-36. [PubMed Link Image]
  4. Herz J, Hamann U, Rogne S, Myklebost O, Gausepohl H, Stanley KK: Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor. EMBO J. 1988 Dec 20;7(13):4119-27. [PubMed Link Image]
  5. Van Leuven F, Stas L, Hilliker C, Lorent K, Umans L, Serneels L, Overbergh L, Torrekens S, Moechars D, De Strooper B, et al.: Structure of the gene (LRP1) coding for the human alpha 2-macroglobulin receptor lipoprotein receptor-related protein. Genomics. 1994 Nov 1;24(1):78-89. [PubMed Link Image]
  6. Van Leuven F, Stas L, Thiry E, Nelissen B, Miyake Y: Strategy to sequence the 89 exons of the human LRP1 gene coding for the lipoprotein receptor related protein: identification of one expressed mutation among 48 polymorphisms. Genomics. 1998 Sep 1;52(2):138-44. [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 3839
Target 11 Name Phytanoyl-CoA dioxygenase, peroxisomal
Target 11 Synonyms
  1. EC 1.14.11.18
  2. PhyH
  3. Phytanic acid oxidase
  4. Phytanoyl-CoA alpha-hydroxylase
  5. Phytanoyl-CoA dioxygenase, peroxisomal precursor
Target 11 Gene Name PHYH
Target 11 Protein Sequence >Phytanoyl-CoA dioxygenase, peroxisomal
MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKF
YEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITK
VQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHY
FPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYE
ENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENI
EKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL
Target 11 Number of Residues 343
Target 11 Molecular Weight 38539
Target 11 Theoretical pI 8.65
Target 11 GO Classification Not Available
Target 11 General Function Not Available
Target 11 Specific Function Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA
Target 11 Pathways Not Available
Target 11 Reactions
  • phytanoyl-CoA + 2-oxoglutarate + O2 = 2-hydroxyphytanoyl-CoA + succinate + CO2
Target 11 Pfam Domain Function
Target 11 Signals
  • None
Target 11 Transmembrane Regions
  • None
Target 11 Essentiality Non-Essential
Target 11 GenBank ID Protein 2564671 Link Image
Target 11 UniProtKB/Swiss-Prot ID O14832 Link Image
Target 11 UniProtKB/Swiss-Prot Entry Name PAHX_HUMAN Link Image
Target 11 PDB ID Not Available
Target 11 Cellular Location
  • Peroxisome
Target 11 Gene Sequence >1017 bp
ATGGAGCAGCTTCGCGCCGCCGCCCGTCTGCAGATTGTTCTGGGCCACCTCGGCCGCCCC
TCGGCCGGGGCTGTCGTAGCTCATCCCACTTCAGGGACTATTTCCTCTGCCAGTTTCCAT
CCTCAACAATTCCAGTATACTCTGGATAATAATGTTCTAACCCTGGAACAGAGAAAATTT
TATGAAGAAAATGGGTTTCTAGTAATCAAAAATCTTGTACCTGATGCCGATATTCAACGC
TTTCGGAATGAGTTTGAAAAAATCTGCAGAAAGGAGGTGAAACCATTAGGATTAACAGTA
ATGAGAGATGTGACCATTTCGAAATCCGAATATGCTCCAAGTGAGAAGATGATCACGAAG
GTCCAGGATTTCCAGGAAGATAAGGAGCTCTTCAGATACTGCACTCTCCCCGAGATTCTG
AAATATGTGGAGTGCTTCACTGGACCTAATATTATGGCCATGCACACAATGTTGATAAAC
AAACCTCCAGATTCTGGCAAGAAGACGTCCCGTCACCCCCTGCACCAGGACCTGCACTAT
TTCCCCTTCAGGCCCAGCGATCTCATCGTTTGCGCCTGGACGGCGATGGAGCACATCAGC
CGGAACAACGGCTGTCTGGTTGTGCTCCCAGGCACGCACAAGGGCTCCCTGAAGCCCCAC
GATTACCCCAAGTGGGAGGGGGGAGTTAACAAAATGTTCCACGGGATCCAGGACTACGAG
GAAAACAAGGCCCGGGTGCACCTGGTGATGGAGAAGGGCGACACTGTTTTCTTCCATCCT
TTGCTCATCCACGGATCTGGTCAGAATAAAACCCAGGGATTCCGGAAGGCAATTTCCTGC
CATTTCGCCAGTGCCGATTGCCACTACATTGACGTGAAGGGCACCAGTCAAGAAAACATC
GAGAAGGAAGTTGTAGGAATAGCACATAAATTCTTTGGAGCTGAAAATAGCGTGAACTTG
AAGGATATTTGGATGTTTCGAGCTCGACTTGTGAAAGGAGAAAGAACCAATCTTTGA
Target 11 GenBank Gene ID
Target 11 GeneCard ID PHYH Link Image
Target 11 GenAtlas ID PHYH Link Image
Target 11 HGNC ID HGNC:8940 Link Image
Target 11 Chromosome Location 10
Target 11 Locus 10pter-p11.2
Target 11 SNPs SNPJam Report Link Image
Target 11 General References
  1. Chambraud B, Radanyi C, Camonis JH, Rajkowski K, Schumacher M, Baulieu EE: Immunophilins, Refsum disease, and lupus nephritis: the peroxisomal enzyme phytanoyl-COA alpha-hydroxylase is a new FKBP-associated protein. Proc Natl Acad Sci U S A. 1999 Mar 2;96(5):2104-9. [PubMed Link Image]
  2. Lee ZH, Kim H, Ahn KY, Seo KH, Kim JK, Bae CS, Kim KK: Identification of a brain specific protein that associates with a refsum disease gene product, phytanoyl-CoA alpha-hydroxylase. Brain Res Mol Brain Res. 2000 Feb 22;75(2):237-47. [PubMed Link Image]
  3. Jansen GA, Ferdinandusse S, Hogenhout EM, Verhoeven NM, Jakobs C, Wanders RJ: Phytanoyl-CoA hydroxylase deficiency. Enzymological and molecular basis of classical Refsum disease. Adv Exp Med Biol. 1999;466:371-6. [PubMed Link Image]
  4. Jansen GA, Hogenhout EM, Ferdinandusse S, Waterham HR, Ofman R, Jakobs C, Skjeldal OH, Wanders RJ: Human phytanoyl-CoA hydroxylase: resolution of the gene structure and the molecular basis of Refsum's disease. Hum Mol Genet. 2000 May 1;9(8):1195-200. [PubMed Link Image]
  5. Mihalik SJ, Morrell JC, Kim D, Sacksteder KA, Watkins PA, Gould SJ: Identification of PAHX, a Refsum disease gene. Nat Genet. 1997 Oct;17(2):185-9. [PubMed Link Image]
  6. Jansen GA, Ofman R, Ferdinandusse S, Ijlst L, Muijsers AO, Skjeldal OH, Stokke O, Jakobs C, Besley GT, Wraith JE, Wanders RJ: Refsum disease is caused by mutations in the phytanoyl-CoA hydroxylase gene. Nat Genet. 1997 Oct;17(2):190-3. [PubMed Link Image]
Target 11 Drug References
  1. Chen C, Wang Q, Fang X, Xu Q, Chi C, Gu J: Roles of phytanoyl-CoA alpha-hydroxylase in mediating the expression of human coagulation factor VIII. J Biol Chem. 2001 Dec 7;276(49):46340-6. [PubMed Link Image]
  2. 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]
  3. 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 12 [top]
Target 12 ID 3840
Target 12 Name Asialoglycoprotein receptor 2
Target 12 Synonyms
  1. ASGP-R 2
  2. ASGPR 2
  3. Hepatic lectin H2
Target 12 Gene Name ASGR2
Target 12 Protein Sequence >Asialoglycoprotein receptor 2
MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFS
LLALSFNILLLVVICVTGSQSEGHRGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGS
VGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVN
WVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDS
DGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVC
EKRRNATGEVA
Target 12 Number of Residues 316
Target 12 Molecular Weight 35192
Target 12 Theoretical pI 6.34
Target 12 GO Classification
Function
binding
carbohydrate binding
sugar binding
Process
Not Available
Component
cell
membrane
Target 12 General Function Not Available
Target 12 Specific Function Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface
Target 12 Pathways Not Available
Target 12 Reactions Not Available
Target 12 Pfam Domain Function
Target 12 Signals
  • None
Target 12 Transmembrane Regions
  • 59-79
Target 12 Essentiality Non-Essential
Target 12 GenBank ID Protein 179081 Link Image
Target 12 UniProtKB/Swiss-Prot ID P07307 Link Image
Target 12 UniProtKB/Swiss-Prot Entry Name ASGR2_HUMAN Link Image
Target 12 PDB ID Not Available
Target 12 Cellular Location
  • Membrane
Target 12 Gene Sequence >936 bp
ATGGCCAAGGACTTTCAAGATATCCAGCAGCTGAGCTCGGAGGAAAATGACCATCCTTTC
CATCAAGGTGAGGGGCCAGGCACTCGCAGGCTGAATCCCAGGAGAGGAAATCCATTTTTG
AAAGGGCCACCTCCTGCCCAGCCCCTGGCACAGCGTCTCTGCTCCATGGTCTGCTTCAGT
CTGCTTGCCCTGAGCTTCAACATCCTGCTGCTGGTGGTCATCTGTGTGACTGGGTCCCAA
AGTGAGGGTCACAGAGGTGCACAGCTGCAAGCCGAGCTGCGGAGCCTGAAGGAAGCTTTC
AGCAACTTCTCCTCGAGCACCCTGACGGAGGTCCAGGCAATCAGCACCCACGGAGGCAGC
GTGGGTGACAAGATCACATCCCTAGGAGCCAAGCTGGAGAAACAGCAGCAGGACCTGAAA
GCAGATCACGATGCCCTGCTCTTCCATCTGAAGCACTTCCCCGTGGACCTGCGCTTCGTG
GCCTGCCAGATGGAGCTCCTCCACAGCAACGGCTCCCAAAGGACCTGCTGCCCCGTCAAC
TGGGTGGAGCACCAAGGCAGCTGCTACTGGTTCTCTCACTCCGGGAAGGCCTGGGCTGAG
GCGGAGAAGTACTGCCAGCTGGAGAACGCACACCTGGTGGTCATCAACTCCTGGGAGGAG
CAGAAATTCATTGTACAACACACGAACCCCTTCAATACCTGGATAGGTCTCACGGACAGT
GATGGCTCTTGGAAATGGGTGGATGGCACAGACTATAGGCACAACTACAAGAACTGGGCT
GTCACTCAGCCAGATAATTGGCACGGGCACGAGCTGGGTGGAAGTGAAGACTGTGTTGAA
GTCCAGCCGGATGGCCGCTGGAACGATGACTTCTGCCTGCAGGTGTACCGCTGGGTGTGT
GAGAAAAGGCGGAATGCCACCGGCGAGGTGGCCTGA
Target 12 GenBank Gene ID
Target 12 GeneCard ID ASGR2 Link Image
Target 12 GenAtlas ID ASGR2 Link Image
Target 12 HGNC ID HGNC:743 Link Image
Target 12 Chromosome Location 17
Target 12 Locus 17p
Target 12 SNPs SNPJam Report Link Image
Target 12 General References
  1. Pan H, Qin WX, Huo KK, Wan DF, Yu Y, Xu ZG, Hu QD, Gu KT, Zhou XM, Jiang HQ, Zhang PP, Huang Y, Li YY, Gu JR: Cloning, mapping, and characterization of a human homologue of the yeast longevity assurance gene LAG1. Genomics. 2001 Sep;77(1-2):58-64. [PubMed Link Image]
  2. Paietta E, Stockert RJ, Racevskis J: Differences in the abundance of variably spliced transcripts for the second asialoglycoprotein receptor polypeptide, H2, in normal and transformed human liver. Hepatology. 1992 Mar;15(3):395-402. [PubMed Link Image]
  3. Spiess M, Lodish HF: Sequence of a second human asialoglycoprotein receptor: conservation of two receptor genes during evolution. Proc Natl Acad Sci U S A. 1985 Oct;82(19):6465-9. [PubMed Link Image]
Target 12 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 13 [top]
Target 13 ID 3841
Target 13 Name ERGIC-53 protein
Target 13 Synonyms
  1. ER-Golgi intermediate compartment 53 kDa protein
  2. ERGIC-53 protein precursor
  3. Gp58
  4. Intracellular mannose- specific lectin MR60
  5. Lectin, mannose-binding 1
Target 13 Gene Name LMAN1
Target 13 Protein Sequence >ERGIC-53 protein
MAGSRQRGLRARVRPLFCALLLSLGRFVRGDGVGGDPAVALPHRRFEYKYSFKGPHLVQS
DGTVPFWAHAGNAIPSSDQIRVAPSLKSQRGSVWTKTKAAFENWEVEVTFRVTGRGRIGA
DGLAIWYAENQGLEGPVFGSADLWNGVGIFFDSFDNDGKKNNPAIVIIGNNGQIHYDHQN
DGASQALASCQRDFRNKPYPVRAKITYYQNTLTVMINNGFTPDKNDYEFCAKVENMIIPA
QGHFGISAATGGLADDHDVLSFLTFQLTEPGKEPPTPDKEISEKEKEKYQEEFEHFQQEL
DKKKEEFQKGHPDLQGQPAEEIFESVGDRELRQVFEGQNRIHLEIKQLNRQLDMILDEQR
RYVSSLTEEISKRGAGMPGQHGQITQQELDTVVKTQHEILRQVNEMKNSMSETVRLVSGM
QHPGSAGGVYETTQHFIDIKEHLHIVKRDIDNLVQRNMPSNEKPKCPELPPFPSCLSTVH
FIIFVVVQTVLFIGYIMYRSQQEAAAKKFF
Target 13 Number of Residues 518
Target 13 Molecular Weight 57550
Target 13 Theoretical pI 6.76
Target 13 GO Classification
Function
Not Available
Process
Not Available
Component
cell
membrane
Target 13 General Function Not Available
Target 13 Specific Function Mannose-specific lectin. May recognize sugar residues of glycoproteins, glycolipids, or glycosylphosphatidyl inositol anchors and may be involved in the sorting or recycling of proteins, lipids, or both. The LMAN1-MCFD2 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins
Target 13 Pathways Not Available
Target 13 Reactions Not Available
Target 13 Pfam Domain Function
Target 13 Signals
  • 1-30
Target 13 Transmembrane Regions
  • 478-498
Target 13 Essentiality Non-Essential
Target 13 GenBank ID Protein 433938 Link Image
Target 13 UniProtKB/Swiss-Prot ID P49257 Link Image
Target 13 UniProtKB/Swiss-Prot Entry Name LMAN1_HUMAN Link Image
Target 13 PDB ID Not Available
Target 13 Cellular Location
  • Endoplasmic reticulum-Golgi intermediate compartment
Target 13 Gene Sequence >1533 bp
ATGGCGGGATCCAGGCAAAGGGGTCTCCGGGCCAGAGTTCGGCCGCTGTTCTGCGCCTTG
CTGCTGTCACTCGGTCGCTTCGTCCGGGGCGACGGCGTGGGAGGAGACCCCGCGGTCGCG
TTGCCACATCGCCGTTTCGAGTACAAATACAGCTTCAAGGGGCCGCACCTGGTGCAGAGC
GACGGGACCGTGCCCTTCTGGGCCCACGCGGGGAATGCTATTCCAAGTTCAGATCAAATT
CGAGTAGCACCATCTTTAAAAAGCCAAAGAGGCTCAGTGTGGACAAAGACAAAAGCGGCC
TTTGAGAACTGGGAAGTTGAGGTGACATTTCGAGTGACTGGAAGAGGTCGAATTGGAGCT
GATGGCCTAGCAATTTGGTATGCAGAAAATCAAGGCTTGGAGGGCCCTGTGTTTGGATCA
GCTGATCTGTGGAATGGTGTTGGAATATTTTTTGATACTTTTGACAATGATGGAAAGAAA
AATAATCCTGCTATAGTAATTATAGGCAACAATGGACAAATCCATTATGACCATCAAAAT
GACGGGGCTAGTCAAGCTTTGGCAAGTTGCCAGAGGGACTTCCGCAACAAACCCTATCCT
GTCCGAGCAAAGATTACCTATTACCAGAACACACTGACAGTAATGATCAATAATGGCTTT
ACACCAGATAAAAATGATTATGAATTTTGTGCCAAAGTGGAAAATATGATTATCCCTGCA
CAAGGGCATTTTGGAATATCTGCTGCAACTGGAGGTCTTGCAGATGACCATGATGTCCTT
TCTTTTCTGACTTTCCAGTTGACTGAACCTGGAAAAGAGCCGCCCACACCAGATAAAGAA
ATTTCGGAAAAGGAAAAAGAAAAGTATCAGGAGGAATTTGAGCACTTTCAACAAGAATTG
GATAAAAAAAAAGAGGAATTCCAGAAGGGCCACCCCGACCTCCAAGGGCAGCCTGCGGAG
GAAATATTTGAGAGTGTAGGAGATCGAGAGCTAAGACAAGTCTTTGAAGGACAGAATCGT
ATTCATCTTGAAATCAAGCAGCTGAACCGGCAGTTAGATATGATTCTTGATGAACAGAGA
AGATATGTCTCTTCCTTAACAGAGGAAATCTCTAAAAGAGGAGCAGGAATGCCTGGGCAG
CATGGGCAGATTACTCAACAAGAACTGGATACTGTTGTGAAAACTCAGCATGAGATTCTG
AGACAAGTAAATGAAATGAAAAATTCCATGAGTGAAACCGTCAGACTGGTCAGTGGAATG
CAGCACCCTGGCTCTGCTGGAGGCGTCTATGAGACAACACAGCACTTCATTGACATCAAA
GAGCACCTGCACATAGTAAAGAGGGACATAGATAACTTAGTGCAGCGAAATATGCCATCA
AATGAAAAGCCGAAATGCCCAGAACTACCACCATTTCCATCATGTTTGTCTACGGTCCAC
TTCATTATATTTGTTGTGGTGCAAACTGTATTATTCATTGGTTATATCATGTATAGGTCT
CAGCAAGAAGCAGCTGCCAAAAAATTCTTTTGA
Target 13 GenBank Gene ID
Target 13 GeneCard ID LMAN1 Link Image
Target 13 GenAtlas ID LMAN1 Link Image
Target 13 HGNC ID HGNC:6631 Link Image
Target 13 Chromosome Location 18
Target 13 Locus 18q21.3-q22
Target 13 SNPs SNPJam Report Link Image
Target 13 General References
  1. Nichols WC, Terry VH, Wheatley MA, Yang A, Zivelin A, Ciavarella N, Stefanile C, Matsushita T, Saito H, de Bosch NB, Ruiz-Saez A, Torres A, Thompson AR, Feinstein DI, White GC, Negrier C, Vinciguerra C, Aktan M, Kaufman RJ, Ginsburg D, Seligsohn U: ERGIC-53 gene structure and mutation analysis in 19 combined factors V and VIII deficiency families. Blood. 1999 Apr 1;93(7):2261-6. [PubMed Link Image]
  2. Harris RA, Yang A, Stein RC, Lucy K, Brusten L, Herath A, Parekh R, Waterfield MD, O'Hare MJ, Neville MA, Page MJ, Zvelebil MJ: Cluster analysis of an extensive human breast cancer cell line protein expression map database. Proteomics. 2002 Feb;2(2):212-23. [PubMed Link Image]
  3. Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed Link Image]
  4. Arar C, Carpentier V, Le Caer JP, Monsigny M, Legrand A, Roche AC: ERGIC-53, a membrane protein of the endoplasmic reticulum-Golgi intermediate compartment, is identical to MR60, an intracellular mannose-specific lectin of myelomonocytic cells. J Biol Chem. 1995 Feb 24;270(8):3551-3. [PubMed Link Image]
  5. Fiedler K, Simons K: A putative novel class of animal lectins in the secretory pathway homologous to leguminous lectins. Cell. 1994 Jun 3;77(5):625-6. [PubMed Link Image]
  6. Schindler R, Itin C, Zerial M, Lottspeich F, Hauri HP: ERGIC-53, a membrane protein of the ER-Golgi intermediate compartment, carries an ER retention motif. Eur J Cell Biol. 1993 Jun;61(1):1-9. [PubMed Link Image]
Target 13 Drug References
  1. Cunningham MA, Pipe SW, Zhang B, Hauri HP, Ginsburg D, Kaufman RJ: LMAN1 is a molecular chaperone for the secretion of coagulation factor VIII. J Thromb Haemost. 2003 Nov;1(11):2360-7. [PubMed Link Image]
  2. Miao HZ, Sirachainan N, Palmer L, Kucab P, Cunningham MA, Kaufman RJ, Pipe SW: Bioengineering of coagulation factor VIII for improved secretion. Blood. 2004 May 1;103(9):3412-9. Epub 2004 Jan 15. [PubMed Link Image]
  3. [PubMed Link Image]
  4. 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]
  5. 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 14 [top]
Target 14 ID 3842
Target 14 Name Multiple coagulation factor deficiency protein 2
Target 14 Synonyms
  1. Multiple coagulation factor deficiency protein 2 precursor
  2. Neural stem cell-derived neuronal survival protein
Target 14 Gene Name MCFD2
Target 14 Protein Sequence >Multiple coagulation factor deficiency protein 2
MTMRSLLRTPFLCGLLWAFCAPGARAEEPAASFSQPGSMGLDKNTVHDQEHIMEHLEGVI
NKPEAEMSPQELQLHYFKMHDYDGNNLLDGLELSTAITHVHKEEGSEQAPLMSEDELINI
IDGVLRDDDKNNDGYIDYAEFAKSLQ
Target 14 Number of Residues 148
Target 14 Molecular Weight 16391
Target 14 Theoretical pI 4.25
Target 14 GO Classification
Function
binding
ion binding
cation binding
calcium ion binding
Process
Not Available
Component
Not Available
Target 14 General Function Not Available
Target 14 Specific Function The MCFD2-LMAN1 complex forms a specific cargo receptor for the ER-to-Golgi transport of selected proteins
Target 14 Pathways Not Available
Target 14 Reactions Not Available
Target 14 Pfam Domain Function Not Available
Target 14 Signals
  • 1-26
Target 14 Transmembrane Regions
  • None
Target 14 Essentiality Non-Essential
Target 14 GenBank ID Protein 20799383 Link Image
Target 14 UniProtKB/Swiss-Prot ID Q8NI22 Link Image
Target 14 UniProtKB/Swiss-Prot Entry Name MCFD2_HUMAN Link Image
Target 14 PDB ID Not Available
Target 14 Cellular Location
  • Endoplasmic reticulum-Golgi intermediate compartment
Target 14 Gene Sequence >441 bp
ATGACCATGAGATCCCTGCTCAGAACCCCCTTCCTGTGTGGCCTGCTCTGGGCCTTTTGT
GCCCCAGGCGCCAGGGCTGAGGAGCCTGCAGCCAGCTTCTCCCAACCCGGCAGCATGGGC
CTGGATAAGAACACAGTGCACGACCAAGAGCATATCATGGAGCATCTAGAAGGTGTCATC
AACAAACCAGAGGCGGAGATGTCGCCACAAGAATTGCAGCTCCATTACTTCAAAATGCAT
GATTATGATGGCAATAATTTGCTTGATGGCTTAGAACTCTCCACAGCCATCACTCATGTC
CATAAGGAGGAAGGGAGTGAACAGGCACCACTAATGAGTGAAGATGAACTGATTAACATA
ATAGATGGTGTTTTGAGAGATGATGACAAGAACAATGATGGATACATTGACTATGCTGAA
TTTGCAAAATCACTGCAGTAG
Target 14 GenBank Gene ID
Target 14 GeneCard ID MCFD2 Link Image
Target 14 GenAtlas ID MCFD2 Link Image
Target 14 HGNC ID HGNC:18451 Link Image
Target 14 Chromosome Location 2
Target 14 Locus 2p21
Target 14 SNPs SNPJam Report Link Image
Target 14 General References Not Available
Target 14 Drug References
  1. [PubMed Link Image]
  2. 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]
  3. 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.