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CD59 (CD59 molecule, complement regulatory protein)

Written2012-12Rossen M Donev, Martin V Kolev
Institute of Life Science, College of Medicine, Swansea University, Swansea, UK (RMD); MRC Centre for Transplantation, King's College London, Guy's Hospital, London, UK (MVK)

(Note : for Links provided by Atlas : click)


Alias (NCBI)16.3A5
HGNC (Hugo) CD59
HGNC Alias symb16.3A5
HGNC Previous nameMIC11
HGNC Previous nameCD59 antigen p18-20 (antigen identified by monoclonal antibodies 16.3A5, EJ16, EJ30, EL32 and G344)
 CD59 antigen, complement regulatory protein
 CD59 molecule, complement regulatory protein
 CD59 molecule
LocusID (NCBI) 966
Atlas_Id 985
Location 11p13  [Link to chromosome band 11p13]
Location_base_pair Starts at 33703010 and ends at 33736479 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping CD59.png]
Local_order FBOX3, CD59, C11orf91.
  Red line marks the position of the CD59 gene in chromosome 11, p13.
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
CD59 (11p13)::BLOC1S5 (6p24.3)CD59 (11p13)::CD59 (11p13)CD59 (11p13)::COL7A1 (3p21.31)
CD59 (11p13)::FBXO3 (11p13)CD59 (11p13)::NCBP1 (9q22.33)CD59 (11p13)::RBPJ (4p15.2)
H2AFZ (4q23)::CD59 (11p13)MALAT1 (11q13.1)::CD59 (11p13)NOTCH2 (1p12)::CD59 (11p13)
SERPINA3 (14q32.13)::CD59 (11p13)
Note CD59 gene encodes a ubiquitously expressed membrane-bound glycoprotein which inhibits complement system. More specifically, CD59 binds complement C8 and/or C9 during the assembly of the membrane attack complex, thus protecting self-cells from damage caused by the activation of the terminal pathway of complement cascade (Bubeck et al., 2011; Walport, 2001).


  CD59 gene consists of 7 exons and 6 introns spanning 1 to 33470bp of DNA (NCBI Reference Sequence: NG_008057.1) from 11p13 and includes a 5'-/3'- non-coding regions. The position of exons is: 1..98 (exon 1), 2870..2985 (exon 2), 5012..5056 (exon 3), 13528..13563 (exon 4), 13753..13844 (exon 5a), 13753..13909 (exon 5b), 13753..14101 (exon 5c), 14017..14101 (exon 5d), 19009..19110 (exon 6), and 26137..33470 (exon 7). Highlighted in red is the protein coding sequence from exons 5c/5d, 6 and 7 (14035..26354).
Description NCBI Reference Sequence: NG_008057.1.
Transcription - Total range: NG_008057.1
- exon 1: (1..98); total length: 98; strand: plus
- exon 2: (2870..2985); total length: 116; strand: plus
- exon 3: (5012..5056); total length: 45; strand: plus
- exon 4: (13528..13563); total length: 36; strand: plus
- exon 5a: (13753..13844); total length: 92; strand: plus
- exon 5b :(13753..13909); total length: 157; strand: plus
- exon 5c: (13753..14101); total length: 349; strand: plus
- exon 5d: (14017..14101); total length: 85; strand: plus
- exon 6: (19009..19110); total length: 102; strand: plus
- exon 7: (26137..33470); total length: 7,334; strand: plus.
Transcription results in 22 different mRNAs (20 alternatively spliced variants and 2 unspliced forms). Despite the very high number of different CD59 transcripts, most of them vary at their 5' and/or 3' ends and encode a unique CD59 protein. However, different splicing variants have alternative promoters and stabilising sequences which is likely to affect the expression level of the protein.


  Sequence of CD59 protein. CD59 contains 10 cystein residues involved in 5 disulphide bonds creating 5 loop structures. First three helical loops at the N-terminus form the hydrophobic core of CD59. Detailed information on CD59 protein structure can be obtained in works published by Bubeck et al. (Bubeck et al., 2011) and Huang et al. (Huang et al., 2007).
Description CD59 is a 128aa-long protein. No polymorphisms have been described in the protein coding sequence of the CD59 gene. All transcription variants of CD59 result in the synthesis of a single CD59 protein with molecular mass between 18 and 22 kDa, depending on the level of glycosylation. CD59 has sites for both N- and O-glycosylation.
Expression CD59 is expressed in all organs and in almost all cell types. It is essential to protect cells from self-destruction by complement-mediated lysis. The highest expression in humans has been detected in cardiomyocytes and smooth muscles (Su et al., 2004). Some nucleated blood cells (CD14 monocytes, T cells) either lack CD59 expression or express it very low which makes them highly susceptible to complement lysis.
Localisation CD59 is expressed on the surface of cells. It is attached to the cellular membrane via a glycosylphosphatidylinositol tail (GPI-anchored molecule). In urine, CD59 can be found as soluble protein.
Function The major and well-studied role of CD59 protein is to protect cells from self-destruction by our complement system. CD59 is the only membrane-bound inhibitor of the terminal pathway of complement cascade. However, in more recent years, some other functions of CD59 were described. CD59 was found to attenuate angiogenesis by preventing the complement-mediated lysis of newly grown blood vessels (Ekdahl et al., 2006). In addition, it was found that via CD59, the LPS signal is transduced into the nucleus via NF-kappaB activation inducing cytokine generation (Yamamoto et al., 2003).
Homology CD59 protein does not show significant homology with other proteins. However, there is a high cross-primates homology for CD59. Human CD59 has 84% homology with CD59 in Macaca fascicularis and 91% homology in Pongo abelii (BLAST search). Homology between human CD59 protein and CD59 in rodents, however, is less than 50% (BLAST analysis).


Somatic No polymorphisms have been described for CD59 gene which affect the protein sequence. However, analysis of the sequence of the human CD59 gene revealed the presence of a (GT)19 dinucleotide repeat ~800bp upstream from exon 1 (Nöthen and Dewald, 1995). This polymorphism might affect expression and/or stability of CD59 transcripts, however, there is no experimental information on this matter.
A mutation in another gene, PIGA gene, however, indirectly results in lack of CD59 on red blood cells (RBCs). This condition is called paroxysmal nocturnal haemoglobinuria (PNH) and is a clonal disorder of RBCs. As a result of defective PIGA function, affected RBCs lack all GPI-linked membrane proteins, including CD59. The lack of CD59 renders PNH-RBCs susceptible to autologous complement lysis (Botto et al., 2009).

Implicated in

Entity Paroxysmal nocturnal hemoglobinuria (PNH)
Note Decrease or absence of glycosylphosphatidylinositol-anchored molecules from the surface of the affected cells, such as CD59 (and CD55), resulting in chronic intravascular hemolysis, cytopenia and increased tendency to thrombosis, venous thrombosis, deficient hematopoiesis and, rarely, leukemic conversion.
Disease PNH involves the defective synthesis of a glycosylphosphatidylinositol (GPI) anchor that is used by certain surface proteins for tethering to the cell membrane, such as CD59 (Meri and Jarva, 1998).
Somatic mutations in the X-linked gene PIGA (GPI complementation group A) which encodes a protein required in the biosynthesis of GPI molecules, have been strongly implicated in the pathogenesis of PNH (Rosti, 2000).
Prognosis Poor.
Oncogenesis Possible association between paroxysmal nocturnal hemoglobinuria phenotype and lymphoproliferative syndromes (Meletis et al., 2001).
Entity Alzheimer's disease (AD)
Note It was demonstrated at both protein and mRNA levels that CD59 expression in frontal cortex and hippocampus in AD brains was significantly decreased when compared with normal age matched non-demented individuals, supporting the hypothesis that AD brains are particularly vulnerable to complement-mediated neuronal death (Yang et al., 2000).
Disease AD is a neurodegenerative disease that causes changes in brain function. AD usually affects people over the age of 65 years, with a progressive decline in memory, thinking, language and learning capacity. Age is the strongest predictor for the development and progression of AD (Tanna, 2004).
Prognosis AD is incurable. It leads to death within an average of eight years after diagnosis, the last three of which are typically spent in an institution.
Cytogenetics The molecular mechanisms and hypotheses of AD can be incredibly complex. One of the key events leading to AD appears to be the formation of a peptide (protein) known as amyloid beta (beta amyloid, Aβ), which clusters into amyloid plaques (senile plaques) on the blood vessels and on the outside surface of neurons of the brain. This plaques have been shown to activate the complement system (Kolev et al., 2009).
Entity Breast cancer
Disease Human breast cancer cells are protected from complement-dependent lysis (CDC) by overexpression of CD59 (Yu et al., 1999). It has been shown in numerous studies that inhibition/neutralization of CD59 on breast tumour cells increases tumour killing by complement system both in vivo and in vitro.
Prognosis A recent comparative proteomics study provided novel insights into key proteins associated with the metastatic potential of breast cancer cells and identified CD59 as a marker for breast cancer aggressiveness (Terp et al., 2012).
Oncogenesis Overexpression of CD59 on the surface of tumour cells confers resistance to CDC which has been suggested to result in tumour growth (Chen et al., 2000; Donev et al., 2006).
Entity Ovarian cancer
Disease CD59 is strongly expressed in the ovarian tumor tissues and their associated cell lines cells in all 28 benign and malignant tumors examined (Bjørge et al., 1997). Neutralization of CD59 with an anti-CD59 monoclonal antibody or inhibition of cd59 expression by siRNA significantly enhances CDC of the ovarian cell lines (Kolev et al., 2011).
Prognosis Significant reduced levels of CD59 were detected in the urine of patients with ovarian carcinoma compared to the control subjects (Abdullah-Soheimi et al., 2010). Thus, CD59 can be used as a biomarker in the development of noninvasive assays for diagnosis and screening for ovarian carcinoma.
Oncogenesis It has been demonstrated that overexpression of CD59 on cancer cell surface promotes tumour growth in vitro and in vivo by protecting them from complement lysis (Chen et al., 2000; Donev et al., 2006).
Entity Various cancers
Note Complement is one of the main mediators of antibody-based cancer therapy via the CDC effect. Tumour cells overexpress CD59 which plays a critical role in resistance to CDC and monoclonal antibody-therapy for treatment of cancer (Juhl et al., 1997; Yan et al., 2008).
Disease CD59 is overexpress on the surface of different tumour types and their associated cell lines - colorectal cancer (Thorsteinsson et al., 1998), B-cell leukemias (Treon et al., 2001), neuroblastoma (Donev et al., 2008), prostate cancer (Jarvis et al., 1997), malignant melanoma (Weichenthal et al., 1999), lung carcinoma (Varsano et al., 1998), etc.
Prognosis In general, overexpression of CD59 on tumour surface is associated with poor prognosis.
Oncogenesis It has been demonstrated that overexpression of CD59 on cell surface promotes tumour growth in vitro and in vivo by protecting them from complement lysis (Chen et al., 2000; Donev et al., 2006).
Entity Diabetes
Note Glycation was shown to inhibit CD59 function. In presence of glycation on CD59 it loses its MAC-inhibitory function and results in vascular proliferavative complications like diabetes (Davies et al., 2005). Loss of functional CD59 in hyperglycaemics contributes to their susceptibility to lysis by complement. Thus, it was suggested that glycation-induced inactivation of CD59 is a factor contributing to anaemia in type I diabetes. It is hypothesized that glycation near residue K41 and W40, two highly conserved amino acids essential for the CD59 function, inhibits CD59 function (Davies et al., 2005).
Disease Diabetes is a disease due to an increased level in glucose, which results in glycation and impairment of protein function. Glycation is when a sugar molecule binds a protein or a lipid molecule without the control of an enzyme.
Entity Age-related macular degeneration (AMD)
Note Immunohistochemical studies have localized activated complement components, including the membrane attack complex (MAC) in retinal pigment epithelium (RPE) and drusen in the eyes of patients with AMD (Johnson et al., 2000). CD59 protects autologous cell killing by preventing the formation of lytic MAC on the cell membrane (Meri et al., 1990). The expression of CD59 was found to be significantly lower on CD14(+) monocytes in patients with neovascular AMD compared with controls (Singh et al., 2012). Introduction of human CD59 using adenoviral vectors as a possible therapeutic strategy has been proposed (Ramo et al., 2008).
Disease Molecular basis for AMD is not well understood, a growing body of evidence has recently implicated inflammatory processes, specifically the complement system, in the pathogenesis of this disease (Johnson et al., 2000).
Prognosis AMD is the leading cause of blindness among the elderly in industrialized nations (Klein et al., 2008).
Entity Major depression
Note Expression of CD59 has been found significantly inhibited in an animal model of major depression (Pajer et al., 2012). This suggests that neurons become more susceptible to complement-mediated damage.
Disease Early-onset major depressive disorder (MDD) is a serious psychiatric condition occurring in people under 25 years of age. Early onset of MDD predicts greater familial risk, suggesting a substantial genetic etiology. Approximately 1% of the population of 12 years has MDD, but rates increase to 17-25% by late adolescence and young adulthood (Pajer et al., 2012).


Note Chromosomal in situ hybridization and pulsed field gel electrophoresis mapped the CD59 gene to 11p13, distal to the breakpoint of acute TCL2 (T-Cell Leukemia) and proximal to the Wilms tumor gene (WT1) (Heckl-Ostreicher et al., 1993).


Patients with ovarian carcinoma excrete different altered levels of urine CD59, kininogen-1 and fragments of inter-alpha-trypsin inhibitor heavy chain H4 and albumin.
Abdullah-Soheimi SS, Lim BK, Hashim OH, Shuib AS.
Proteome Sci. 2010 Nov 17;8:58. doi: 10.1186/1477-5956-8-58.
PMID 21083881
Complement-regulatory proteins in ovarian malignancies.
Bjorge L, Hakulinen J, Wahlstrom T, Matre R, Meri S.
Int J Cancer. 1997 Jan 6;70(1):14-25.
PMID 8985085
Complement in human diseases: Lessons from complement deficiencies.
Botto M, Kirschfink M, Macor P, Pickering MC, Wurzner R, Tedesco F.
Mol Immunol. 2009 Sep;46(14):2774-83. doi: 10.1016/j.molimm.2009.04.029. Epub 2009 May 28. (REVIEW)
PMID 19481265
Structure of human complement C8, a precursor to membrane attack.
Bubeck D, Roversi P, Donev R, Morgan BP, Llorca O, Lea SM.
J Mol Biol. 2011 Jan 14;405(2):325-30. doi: 10.1016/j.jmb.2010.10.031. Epub 2010 Nov 10.
PMID 21073882
CD59 expressed on a tumor cell surface modulates decay-accelerating factor expression and enhances tumor growth in a rat model of human neuroblastoma.
Chen S, Caragine T, Cheung NK, Tomlinson S.
Cancer Res. 2000 Jun 1;60(11):3013-8.
PMID 10850450
Glycation of CD59 impairs complement regulation on erythrocytes from diabetic subjects.
Davies CS, Harris CL, Morgan BP.
Immunology. 2005 Feb;114(2):280-6.
PMID 15667573
p53 regulates cellular resistance to complement lysis through enhanced expression of CD59.
Donev RM, Cole DS, Sivasankar B, Hughes TR, Morgan BP.
Cancer Res. 2006 Feb 15;66(4):2451-8.
PMID 16489052
Modulation of CD59 expression by restrictive silencer factor-derived peptides in cancer immunotherapy for neuroblastoma.
Donev RM, Gray LC, Sivasankar B, Hughes TR, van den Berg CW, Morgan BP.
Cancer Res. 2008 Jul 15;68(14):5979-87. doi: 10.1158/0008-5472.CAN-07-6828.
PMID 18632654
Possible immunoprotective and angiogenesis-promoting roles for malignant cell-derived prostasomes: a new paradigm for prostatic cancer?
Ekdahl KN, Ronquist G, Nilsson B, Babiker AA.
Adv Exp Med Biol. 2006;586:107-19. (REVIEW)
PMID 16893068
Localization of the human CD59 gene by fluorescence in situ hybridization and pulsed-field gel electrophoresis.
Heckl-Ostreicher B, Ragg S, Drechsler M, Scherthan H, Royer-Pokora B.
Cytogenet Cell Genet. 1993;63(3):144-6.
PMID 7683594
Crystal structure of CD59: implications for molecular recognition of the complement proteins C8 and C9 in the membrane-attack complex.
Huang Y, Fedarovich A, Tomlinson S, Davies C.
Acta Crystallogr D Biol Crystallogr. 2007 Jun;63(Pt 6):714-21. Epub 2007 May 15.
PMID 17505110
Expression and function of the complement membrane attack complex inhibitor protectin (CD59) in human prostate cancer.
Jarvis GA, Li J, Hakulinen J, Brady KA, Nordling S, Dahiya R, Meri S.
Int J Cancer. 1997 Jun 11;71(6):1049-55.
PMID 9185710
A potential role for immune complex pathogenesis in drusen formation.
Johnson LV, Ozaki S, Staples MK, Erickson PA, Anderson DH.
Exp Eye Res. 2000 Apr;70(4):441-9.
PMID 10865992
Frequent expression of complement resistance factors CD46, CD55, and CD59 on gastrointestinal cancer cells limits the therapeutic potential of monoclonal antibody 17-1A.
Juhl H, Helmig F, Baltzer K, Kalthoff H, Henne-Bruns D, Kremer B.
J Surg Oncol. 1997 Mar;64(3):222-30.
PMID 9121154
The epidemiology of retinal reticular drusen.
Klein R, Meuer SM, Knudtson MD, Iyengar SK, Klein BE.
Am J Ophthalmol. 2008 Feb;145(2):317-326. Epub 2007 Nov 28.
PMID 18045568
Complement in cancer and cancer immunotherapy.
Kolev M, Towner L, Donev R.
Arch Immunol Ther Exp (Warsz). 2011 Dec;59(6):407-19. doi: 10.1007/s00005-011-0146-x. Epub 2011 Sep 30. (REVIEW)
PMID 21960413
Implication of complement system and its regulators in Alzheimer's disease.
Kolev MV, Ruseva MM, Harris CL, Morgan BP, Donev RM.
Curr Neuropharmacol. 2009 Mar;7(1):1-8. doi: 10.2174/157015909787602805.
PMID 19721814
Detection of CD55- and/or CD59-deficient red cell populations in patients with lymphoproliferative syndromes.
Meletis J, Terpos E, Samarkos M, Meletis C, Apostolidou E, Komninaka V, Korovesis K, Mavrogianni D, Boutsis D, Variami E, Viniou N, Konstantopoulos K, Loukopoulos D.
Hematol J. 2001;2(1):33-7.
PMID 11920231
Complement regulation.
Meri S, Jarva H.
Vox Sang. 1998;74 Suppl 2:291-302. (REVIEW)
PMID 9704459
Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers.
Meri S, Morgan BP, Davies A, Daniels RH, Olavesen MG, Waldmann H, Lachmann PJ.
Immunology. 1990 Sep;71(1):1-9.
PMID 1698710
Dinucleotide repeat polymorphism at the human CD59 locus.
Nothen MM, Dewald G.
Clin Genet. 1995 Mar;47(3):165-6.
PMID 7543386
Evaluation of adenovirus-delivered human CD59 as a potential therapy for AMD in a model of human membrane attack complex formation on murine RPE.
Ramo K, Cashman SM, Kumar-Singh R.
Invest Ophthalmol Vis Sci. 2008 Sep;49(9):4126-36. doi: 10.1167/iovs.08-2025. Epub 2008 May 16.
PMID 18487376
The molecular basis of paroxysmal nocturnal hemoglobinuria.
Rosti V.
Haematologica. 2000 Jan;85(1):82-7. (REVIEW)
PMID 10629597
Altered expression of CD46 and CD59 on leukocytes in neovascular age-related macular degeneration.
Singh A, Faber C, Falk M, Nissen MH, Hviid TV, Sorensen TL.
Am J Ophthalmol. 2012 Jul;154(1):193-199.e2. doi: 10.1016/j.ajo.2012.01.036. Epub 2012 Apr 27.
PMID 22541656
A gene atlas of the mouse and human protein-encoding transcriptomes.
Su AI, Wiltshire T, Batalov S, Lapp H, Ching KA, Block D, Zhang J, Soden R, Hayakawa M, Kreiman G, Cooke MP, Walker JR, Hogenesch JB.
Proc Natl Acad Sci U S A. 2004 Apr 20;101(16):6062-7. Epub 2004 Apr 9.
PMID 15075390
Alzheimer's disease - Opportunities to address pharmaceutical gaps (a background paper).
Tanna S.
In: Kaplan, W., Laing, R. Eds., Priority Medicines for Europe and the World. World Health Organization, Department of Essential Drugs and Medicines Policy. 2004; pp. 3-6.
Identification of markers associated with highly aggressive metastatic phenotypes using quantitative comparative proteomics.
Terp MG, Lund RR, Jensen ON, Leth-Larsen R, Ditzel HJ.
Cancer Genomics Proteomics. 2012 Sep-Oct;9(5):265-73.
PMID 22990106
The complement regulatory proteins CD46 and CD59, but not CD55, are highly expressed by glandular epithelium of human breast and colorectal tumour tissues.
Thorsteinsson L, O'Dowd GM, Harrington PM, Johnson PM.
APMIS. 1998 Sep;106(9):869-78.
PMID 9808413
Tumor cell expression of CD59 is associated with resistance to CD20 serotherapy in patients with B-cell malignancies.
Treon SP, Mitsiades C, Mitsiades N, Young G, Doss D, Schlossman R, Anderson KC.
J Immunother. 2001 May-Jun;24(3):263-71.
PMID 11394505
Human lung cancer cell lines express cell membrane complement inhibitory proteins and are extremely resistant to complement-mediated lysis; a comparison with normal human respiratory epithelium in vitro, and an insight into mechanism(s) of resistance.
Varsano S, Rashkovsky L, Shapiro H, Ophir D, Mark-Bentankur T.
Clin Exp Immunol. 1998 Aug;113(2):173-82.
PMID 9717965
Complement. First of two parts.
Walport MJ.
N Engl J Med. 2001 Apr 5;344(14):1058-66. (REVIEW)
PMID 11287977
Expression of complement regulator proteins in primary and metastatic malignant melanoma.
Weichenthal M, Siemann U, Neuber K, Breitbart EW.
J Cutan Pathol. 1999 May;26(5):217-21.
PMID 10408345
Lipopolysaccharide signal transduction in oral keratinocytes--involvement of CD59 but not CD14.
Yamamoto T, Nakane T, Doi S, Osaki T.
Cell Signal. 2003 Sep;15(9):861-9.
PMID 12834811
The role of membrane complement regulatory proteins in cancer immunotherapy.
Yan J, Allendorf DJ, Li B, Yan R, Hansen R, Donev R.
Adv Exp Med Biol. 2008;632:159-74. (REVIEW)
PMID 19025121
Deficiency of complement defense protein CD59 may contribute to neurodegeneration in Alzheimer's disease.
Yang LB, Li R, Meri S, Rogers J, Shen Y.
J Neurosci. 2000 Oct 15;20(20):7505-9.
PMID 11027207
Protection of human breast cancer cells from complement-mediated lysis by expression of heterologous CD59.
Yu J, Caragine T, Chen S, Morgan BP, Frey AB, Tomlinson S.
Clin Exp Immunol. 1999 Jan;115(1):13-8.
PMID 9933415


This paper should be referenced as such :
Donev, RM ; Kolev, MV
CD59 (CD59 molecule, complement regulatory protein)
Atlas Genet Cytogenet Oncol Haematol. 2013;17(6):391-395.
Free journal version : [ pdf ]   [ DOI ]

External links


HGNC (Hugo)CD59   1689
LRG (Locus Reference Genomic)LRG_41
Entrez_Gene (NCBI)CD59    CD59 molecule (CD59 blood group)
Aliases16.3A5; 1F5; EJ16; EJ30; 
EL32; G344; HRF-20; HRF20; MAC-IP; MACIF; MEM43; MIC11; MIN1; MIN2; MIN3; MIRL; MSK21; p18-20
GeneCards (Weizmann)CD59
Ensembl hg19 (Hinxton)ENSG00000085063 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000085063 [Gene_View]  ENSG00000085063 [Sequence]  chr11:33703010-33736479 [Contig_View]  CD59 [Vega]
ICGC DataPortalENSG00000085063
TCGA cBioPortalCD59
AceView (NCBI)CD59
Genatlas (Paris)CD59
SOURCE (Princeton)CD59
Genetics Home Reference (NIH)CD59
Genomic and cartography
GoldenPath hg38 (UCSC)CD59  -     chr11:33703010-33736479 -  11p13   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)CD59  -     11p13   [Description]    (hg19-Feb_2009)
GoldenPathCD59 - 11p13 [CytoView hg19]  CD59 - 11p13 [CytoView hg38]
Genome Data Viewer NCBICD59 [Mapview hg19]  
OMIM107271   612300   
Gene and transcription
Genbank (Entrez)AI147924 AK128571 AK309894 AK311778 AL037045
RefSeq transcript (Entrez)NM_000611 NM_001127223 NM_001127225 NM_001127226 NM_001127227 NM_203329 NM_203330 NM_203331
Consensus coding sequences : CCDS (NCBI)CD59
Gene ExpressionCD59 [ NCBI-GEO ]   CD59 [ EBI - ARRAY_EXPRESS ]   CD59 [ SEEK ]   CD59 [ MEM ]
Gene Expression Viewer (FireBrowse)CD59 [ Firebrowse - Broad ]
GenevisibleExpression of CD59 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)966
GTEX Portal (Tissue expression)CD59
Human Protein AtlasENSG00000085063-CD59 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
UniProt/SwissProtP13987   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP13987  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP13987
Domaine pattern : Prosite (Expaxy)LY6_UPAR (PS00983)   
Domains : Interpro (EBI)CD59_antigen_CS    CD59_glyco    LY6_UPA_recep-like   
Domain families : Pfam (Sanger)UPAR_LY6 (PF00021)   
Domain families : Pfam (NCBI)pfam00021   
Domain families : Smart (EMBL)LU (SM00134)  
Conserved Domain (NCBI)CD59
PDB (RSDB)1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
PDB Europe1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
PDB (PDBSum)1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
PDB (IMB)1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
Structural Biology KnowledgeBase1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
SCOP (Structural Classification of Proteins)1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
CATH (Classification of proteins structures)1CDQ    1CDR    1CDS    1ERG    1ERH    2J8B    2OFS    2UWR    2UX2    4BIK    5IMT    5IMY   
AlphaFold pdb e-kbP13987   
Human Protein Atlas [tissue]ENSG00000085063-CD59 [tissue]
Protein Interaction databases
IntAct (EBI)P13987
Ontologies - Pathways
Ontology : AmiGOGolgi membrane  complement binding  negative regulation of activation of membrane attack complex  protein binding  extracellular space  endoplasmic reticulum membrane  plasma membrane  plasma membrane  focal adhesion  endoplasmic reticulum to Golgi vesicle-mediated transport  cell surface receptor signaling pathway  blood coagulation  cell surface  ER to Golgi transport vesicle membrane  membrane  transport vesicle  regulation of complement activation  regulation of complement activation  anchored component of external side of plasma membrane  vesicle  endoplasmic reticulum-Golgi intermediate compartment membrane  specific granule membrane  neutrophil degranulation  COPII vesicle coating  extracellular exosome  tertiary granule membrane  regulation of complement-dependent cytotoxicity  
Ontology : EGO-EBIGolgi membrane  complement binding  negative regulation of activation of membrane attack complex  protein binding  extracellular space  endoplasmic reticulum membrane  plasma membrane  plasma membrane  focal adhesion  endoplasmic reticulum to Golgi vesicle-mediated transport  cell surface receptor signaling pathway  blood coagulation  cell surface  ER to Golgi transport vesicle membrane  membrane  transport vesicle  regulation of complement activation  regulation of complement activation  anchored component of external side of plasma membrane  vesicle  endoplasmic reticulum-Golgi intermediate compartment membrane  specific granule membrane  neutrophil degranulation  COPII vesicle coating  extracellular exosome  tertiary granule membrane  regulation of complement-dependent cytotoxicity  
Pathways : KEGGComplement and coagulation cascades    Hematopoietic cell lineage   
REACTOMEP13987 [protein]
REACTOME PathwaysR-HSA-977606 [pathway]   
NDEx NetworkCD59
Atlas of Cancer Signalling NetworkCD59
Wikipedia pathwaysCD59
Orthology - Evolution
GeneTree (enSembl)ENSG00000085063
Phylogenetic Trees/Animal Genes : TreeFamCD59
Homologs : HomoloGeneCD59
Homology/Alignments : Family Browser (UCSC)CD59
Gene fusions - Rearrangements
Fusion Cancer (Beijing)CD59 [11p13]  -  COL7A1 [3p21.31]  [FUSC002407]
Fusion : QuiverCD59
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerCD59 [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)CD59
Exome Variant ServerCD59
GNOMAD BrowserENSG00000085063
Varsome BrowserCD59
ACMGCD59 variants
Genomic Variants (DGV)CD59 [DGVbeta]
DECIPHERCD59 [patients]   [syndromes]   [variants]   [genes]  
CONAN: Copy Number AnalysisCD59 
ICGC Data PortalCD59 
TCGA Data PortalCD59 
Broad Tumor PortalCD59
OASIS PortalCD59 [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICCD59  [overview]  [genome browser]  [tissue]  [distribution]  
Somatic Mutations in Cancer : COSMIC3DCD59
Mutations and Diseases : HGMDCD59
LOVD (Leiden Open Variation Database)[gene] [transcripts] [variants]
DgiDB (Drug Gene Interaction Database)CD59
DoCM (Curated mutations)CD59
CIViC (Clinical Interpretations of Variants in Cancer)CD59
NCG (London)CD59
Impact of mutations[PolyPhen2] [Provean] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
OMIM107271    612300   
Genetic Testing Registry CD59
NextProtP13987 [Medical]
Target ValidationCD59
Huge Navigator CD59 [HugePedia]
Clinical trials, drugs, therapy
Protein Interactions : CTDCD59
Pharm GKB GenePA26228
Clinical trialCD59
canSAR (ICR)CD59
DataMed IndexCD59
PubMed241 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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indexed on : Fri Oct 8 21:14:29 CEST 2021

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