UniProt ID | CD59_HUMAN | |
---|---|---|
UniProt AC | P13987 | |
Protein Name | CD59 glycoprotein | |
Gene Name | CD59 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 128 | |
Subcellular Localization |
Cell membrane Lipid-anchor, GPI-anchor. Secreted. Soluble form found in a number of tissues. |
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Protein Description | Potent 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.; The soluble form from urine retains its specific complement binding activity, but exhibits greatly reduced ability to inhibit MAC assembly on cell membranes.. | |
Protein Sequence | MGIQGGSVLFGLLLVLAVFCHSGHSLQCYNCPNPTADCKTAVNCSSDFDACLITKAGLQVYNKCWKFEHCNFNDVTTRLRENELTYYCCKKDLCNFNEQLENGGTSLSEKTVLLLVTPFLAAAWSLHP | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
29 | Phosphorylation | SGHSLQCYNCPNPTA CCCCCCCCCCCCCCC | 13.57 | 19534553 | |
43 | N-linked_Glycosylation | ADCKTAVNCSSDFDA CCCCHHHCCCCCCCE | 19.93 | 8798614 | |
43 | N-linked_Glycosylation | ADCKTAVNCSSDFDA CCCCHHHCCCCCCCE | 19.93 | 9054419 | |
63 | Acetylation | AGLQVYNKCWKFEHC HHHHHCHHCCCCCCC | 24.64 | 25825284 | |
66 | Acetylation | QVYNKCWKFEHCNFN HHCHHCCCCCCCCCC | 50.79 | 21466224 | |
66 | Glycation | QVYNKCWKFEHCNFN HHCHHCCCCCCCCCC | 50.79 | - | |
66 | N-linked_Glycosylation | QVYNKCWKFEHCNFN HHCHHCCCCCCCCCC | 50.79 | 10805801 | |
70 | S-palmitoylation | KCWKFEHCNFNDVTT HCCCCCCCCCCCHHH | 4.97 | 29575903 | |
76 | O-linked_Glycosylation | HCNFNDVTTRLRENE CCCCCCHHHHHHHCC | 14.73 | 55830563 | |
76 | Phosphorylation | HCNFNDVTTRLRENE CCCCCCHHHHHHHCC | 14.73 | 29759185 | |
77 | O-linked_Glycosylation | CNFNDVTTRLRENEL CCCCCHHHHHHHCCC | 27.79 | 55830567 | |
86 | Phosphorylation | LRENELTYYCCKKDL HHHCCCEEEEECHHC | 13.71 | 19534553 | |
87 | Phosphorylation | RENELTYYCCKKDLC HHCCCEEEEECHHCC | 6.02 | 24927040 | |
88 | S-palmitoylation | ENELTYYCCKKDLCN HCCCEEEEECHHCCC | 1.61 | 29575903 | |
89 | S-palmitoylation | NELTYYCCKKDLCNF CCCEEEEECHHCCCH | 3.38 | 29575903 | |
90 | Acetylation | ELTYYCCKKDLCNFN CCEEEEECHHCCCHH | 45.84 | 26051181 | |
90 | 2-Hydroxyisobutyrylation | ELTYYCCKKDLCNFN CCEEEEECHHCCCHH | 45.84 | - | |
90 | Ubiquitination | ELTYYCCKKDLCNFN CCEEEEECHHCCCHH | 45.84 | - | |
91 | Ubiquitination | LTYYCCKKDLCNFNE CEEEEECHHCCCHHH | 41.86 | - | |
102 | GPI-anchor | NFNEQLENGGTSLSE CHHHHHHHCCCCCCH | 63.89 | 8276756 |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
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Oops, there are no upstream regulatory protein records of CD59_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
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Oops, there are no descriptions of PTM sites of CD59_HUMAN !! |
* Distance = the distance between SAP position and PTM sites.
Modified Location | Modification | Variant Position (Distance <= 10) |
Residue Change | SAP | Related Disease | Reference |
---|---|---|---|---|---|---|
Oops, there are no SNP-PTM records of CD59_HUMAN !! |
Kegg Disease | ||||||
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H00106 | Complement regulatory protein defects, including the following six diseases: C1 inhibitor deficiency | |||||
OMIM Disease | ||||||
612300 | Hemolytic anemia, CD59-mediated, with or without polyneuropathy (HACD59) | |||||
Kegg Drug | ||||||
There are no disease associations of PTM sites. | ||||||
DrugBank | ||||||
There are no disease associations of PTM sites. |
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GPI-anchor | |
Reference | PubMed |
"Computational approach for identification and characterization ofGPI-anchored peptides in proteomics experiments."; Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K.,Arizmendi J.M., Jensen O.N., Matthiesen R.; Proteomics 7:1951-1960(2007). Cited for: GPI-ANCHOR AT ASN-102, AND MASS SPECTROMETRY. | |
"Modification-specific proteomics of plasma membrane proteins:identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment."; Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,Brodbeck U., Peck S.C., Jensen O.N.; J. Proteome Res. 5:935-943(2006). Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. | |
"Proteomic analysis of glycosylphosphatidylinositol-anchored membraneproteins."; Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,Jensen O.N.; Mol. Cell. Proteomics 2:1261-1270(2003). Cited for: GPI-ANCHOR [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. | |
"The glycosylation of the complement regulatory protein, humanerythrocyte CD59."; Rudd P.M., Morgan B.P., Wormald M.R., Harvey D.J., van den Berg C.W.,Davis S.J., Ferguson M.A., Dwek R.A.; J. Biol. Chem. 272:7229-7244(1997). Cited for: STRUCTURE OF CARBOHYDRATES, STRUCTURE OF THE GPI-ANCHOR, AND PROTEINSEQUENCE OF N-TERMINUS. | |
"Determination of carboxyl-terminal residue and disulfide bonds ofMACIF (CD59), a glycosyl-phosphatidylinositol-anchored membraneprotein."; Sugita Y., Nakano Y., Oda E., Noda K., Tobe T., Miura N.H., Tomita M.; J. Biochem. 114:473-477(1993). Cited for: GPI-ANCHOR AT ASN-102, AND DISULFIDE BONDS. | |
N-linked Glycosylation | |
Reference | PubMed |
"Molecular basis for a link between complement and the vascularcomplications of diabetes."; Acosta J., Hettinga J., Flueckiger R., Krumrei N., Goldfine A.,Angarita L., Halperin J.; Proc. Natl. Acad. Sci. U.S.A. 97:5450-5455(2000). Cited for: INHIBITION BY GLYCATION, GLYCATION AT LYS-66 AND HIS-69, ANDMUTAGENESIS OF LYS-66 AND HIS-69. | |
"Identification of N-linked glycoproteins in human milk by hydrophilicinteraction liquid chromatography and mass spectrometry."; Picariello G., Ferranti P., Mamone G., Roepstorff P., Addeo F.; Proteomics 8:3833-3847(2008). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-43, AND MASS SPECTROMETRY. | |
"Structural composition and functional characterization of solubleCD59: heterogeneity of the oligosaccharide and glycophosphoinositol(GPI) anchor revealed by laser-desorption mass spectrometricanalysis."; Meri S., Lehto T., Sutton C.W., Tyynelaa J., Baumann M.; Biochem. J. 316:923-935(1996). Cited for: PROTEIN SEQUENCE, MASS SPECTROMETRY, GLYCOSYLATION AT ASN-43, ANDSTRUCTURE OF CARBOHYDRATES. | |
Phosphorylation | |
Reference | PubMed |
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells."; Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.; J. Proteome Res. 8:3852-3861(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29 AND TYR-86, AND MASSSPECTROMETRY. |