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MGP000468

UniProt Annotations

Entry Information
Gene NameCD59 molecule, complement regulatory protein
Protein EntryCD59_HUMAN
UniProt IDP13987
SpeciesHuman
Comments
Comment typeDescription
DiseaseHemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59) [MIM:612300]: An autosomal recessive disorder characterized by infantile onset of chronic hemolysis and a relapsing-remitting polyneuropathy, often exacerbated by infection, and manifested as hypotonia, limb muscle weakness, and hyporeflexia. {ECO:0000269|PubMed:1382994, ECO:0000269|PubMed:23149847}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionPotent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore. This inhibitor appears to be species-specific. Involved in signal transduction for T-cell activation complexed to a protein tyrosine kinase.
FunctionThe soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.
InteractionQ778I9:C (xeno); NbExp=4; IntAct=EBI-297972, EBI-8716052; O35587:TMED10 (xeno); NbExp=5; IntAct=EBI-297972, EBI-4405327; Q15363:TMED2; NbExp=4; IntAct=EBI-297972, EBI-998485;
PtmGlycated. Glycation is found in diabetic subjects, but only at minimal levels in nondiabetic subjects. Glycated CD59 lacks MAC-inhibitory function and confers to vascular complications of diabetes.
PtmN- and O-glycosylated. The N-glycosylation mainly consists of a family of biantennary complex-type structures with and without lactosamine extensions and outer arm fucose residues. Also significant amounts of triantennary complexes (22%). Variable sialylation also present in the Asn-43 oligosaccharide. The predominant O-glycans are mono-sialylated forms of the disaccharide, Gal-beta-1,3GalNAc, and their sites of attachment are probably on Thr-76 and Thr-77. The GPI-anchor of soluble urinary CD59 has no inositol-associated phospholipid, but is composed of seven different GPI-anchor variants of one or more monosaccharide units. Major variants contain sialic acid, mannose and glucosamine. Sialic acid linked to an N-acetylhexosamine- galactose arm is present in two variants. {ECO:0000269|PubMed:18780401, ECO:0000269|PubMed:8670172}.
SimilarityContains 1 UPAR/Ly6 domain. {ECO:0000305}.
Subcellular LocationCell membrane; Lipid-anchor, GPI-anchor. Secreted. Note=Soluble form found in a number of tissues.
SubunitInteracts with T-cell surface antigen CD2. {ECO:0000269|PubMed:1377690}.
Web ResourceName=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/CD59ID985ch11p13.html";
Web ResourceName=CD59base; Note=CD59 mutation db; URL="http://structure.bmc.lu.se/idbase/CD59base/";
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