CD59
entrez
966
canonical
uniprot
P13987
canonical
ensembl
ENSG00000085063
resolver
ensembl
ENSG00000284969
resolver
ensp
ENSP00000340210
resolver
ensp
ENSP00000403511
resolver
ensp
ENSP00000404822
resolver
ensp
ENSP00000410182
resolver
ensp
ENSP00000432942
resolver
ensp
ENSP00000494884
resolver
ensp
ENSP00000498448
resolver
ensp
ENSP00000498879
resolver
genesymbol
CD59
resolver
genesymbol_syn
MIC11
resolver
genesymbol_syn
MIN1
resolver
genesymbol_syn
MIN2
resolver
genesymbol_syn
MIN3
resolver
genesymbol_syn
MSK21
resolver
hgnc
HGNC:1689
resolver
uniprot
E9PR17
resolver
uniprot
Q6FHM9
resolver
uniprot_entry
CD59_HUMAN
resolver
uniprot_entry
Q6FHM9_HUMAN
resolver
uniprot_sec
E9PR17
resolver
amino_acid_sequence
MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP
uniprot
proteins
disease_involvement
DISEASE: Hemolytic 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 variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Potent inhibitor of the complement membrane attack complex (MAC) action, which protects human cells from damage during complement activation (PubMed:11882685, PubMed:1698710, PubMed:2475111, PubMed:2475570, PubMed:2606909, PubMed:9053451). Acts by binding to the beta-haipins of C8 (C8A and C8B) components of the assembling MAC, forming an intermolecular beta-sheet that prevents incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore (PubMed:11882685, PubMed:1698710, PubMed:36797260). {ECO:0000269|PubMed:11882685, ECO:0000269|PubMed:1698710, ECO:0000269|PubMed:2475111, ECO:0000269|PubMed:2475570, ECO:0000269|PubMed:2606909, ECO:0000269|PubMed:36797260, ECO:0000269|PubMed:9053451}.; FUNCTION: The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit complement membrane attack complex (MAC) assembly on cell membranes. {ECO:0000269|PubMed:8670172}.
uniprot
proteins
mass_dalton
14177
uniprot
proteins
mutagenesis
MUTAGEN 29; /note="Y->R: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 33; /note="N->R,Q: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 37; /note="D->R: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 48; /note="F->R: Some loss of function. Some lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 49; /note="D->R: Loss of function. Lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 58; /note="L->E: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 63; /note="K->E: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 65; /note="W->E: Complete loss of function. Lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 66; /note="K->D: No loss of function."; /evidence="ECO:0000269|PubMed:10805801"; MUTAGEN 66; /note="K->Q: Loss of glycation mediated inactivation."; /evidence="ECO:0000269|PubMed:10805801"; MUTAGEN 67; /note="F->K: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 69; /note="H->Q: Loss of glycation mediated inactivation."; /evidence="ECO:0000269|PubMed:10805801"; MUTAGEN 72; /note="F->E: Almost complete loss of function. Lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 78; /note="R->E: Loss of function. Lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 79; /note="L->D: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 81; /note="E->R: Almost complete loss of function. Lysis."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 82; /note="N->K: No loss of function."; /evidence="ECO:0000269|PubMed:9053451"; MUTAGEN 87; /note="Y->R: No loss of function."; /evidence="ECO:0000269|PubMed:9053451
uniprot
proteins
post_translational_modification
PTM: N- 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}.; PTM: Glycated (PubMed:10805801). 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 (PubMed:10805801). {ECO:0000269|PubMed:10805801}.
uniprot
proteins
pubmed
10805801
uniprot
proteins
pubmed
11882685
uniprot
proteins
pubmed
1377690
uniprot
proteins
pubmed
1381503
uniprot
proteins
pubmed
1382994
uniprot
proteins
pubmed
1383553
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16554811
uniprot
proteins
pubmed
1689664
uniprot
proteins
pubmed
1692709
uniprot
proteins
pubmed
1698710
uniprot
proteins
pubmed
17566972
uniprot
proteins
pubmed
18780401
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23149847
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
2475111
uniprot
proteins
pubmed
2475570
uniprot
proteins
pubmed
2476718
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
2606909
uniprot
proteins
pubmed
36797260
uniprot
proteins
pubmed
7512825
uniprot
proteins
pubmed
7520819
uniprot
proteins
pubmed
8276756
uniprot
proteins
pubmed
8670172
uniprot
proteins
pubmed
9053451
uniprot
proteins
pubmed
9054419
uniprot
proteins
pubmed
9235986
uniprot
proteins
sequence_length
128
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:36797260}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:8276756}. Secreted {ECO:0000269|PubMed:8670172}. Note=Localizes to the cell surface (PubMed:36797260). Soluble form found in a number of tissues (PubMed:8670172). {ECO:0000269|PubMed:36797260, ECO:0000269|PubMed:8670172}.
uniprot
proteins