CD59_HUMAN - dbPTM
CD59_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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.
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
29PhosphorylationSGHSLQCYNCPNPTA
CCCCCCCCCCCCCCC
13.5719534553
43N-linked_GlycosylationADCKTAVNCSSDFDA
CCCCHHHCCCCCCCE
19.938798614
43N-linked_GlycosylationADCKTAVNCSSDFDA
CCCCHHHCCCCCCCE
19.939054419
63AcetylationAGLQVYNKCWKFEHC
HHHHHCHHCCCCCCC
24.6425825284
66AcetylationQVYNKCWKFEHCNFN
HHCHHCCCCCCCCCC
50.7921466224
66GlycationQVYNKCWKFEHCNFN
HHCHHCCCCCCCCCC
50.79-
66N-linked_GlycosylationQVYNKCWKFEHCNFN
HHCHHCCCCCCCCCC
50.7910805801
70S-palmitoylationKCWKFEHCNFNDVTT
HCCCCCCCCCCCHHH
4.9729575903
76O-linked_GlycosylationHCNFNDVTTRLRENE
CCCCCCHHHHHHHCC
14.7355830563
76PhosphorylationHCNFNDVTTRLRENE
CCCCCCHHHHHHHCC
14.7329759185
77O-linked_GlycosylationCNFNDVTTRLRENEL
CCCCCHHHHHHHCCC
27.7955830567
86PhosphorylationLRENELTYYCCKKDL
HHHCCCEEEEECHHC
13.7119534553
87PhosphorylationRENELTYYCCKKDLC
HHCCCEEEEECHHCC
6.0224927040
88S-palmitoylationENELTYYCCKKDLCN
HCCCEEEEECHHCCC
1.6129575903
89S-palmitoylationNELTYYCCKKDLCNF
CCCEEEEECHHCCCH
3.3829575903
90AcetylationELTYYCCKKDLCNFN
CCEEEEECHHCCCHH
45.8426051181
902-HydroxyisobutyrylationELTYYCCKKDLCNFN
CCEEEEECHHCCCHH
45.84-
90UbiquitinationELTYYCCKKDLCNFN
CCEEEEECHHCCCHH
45.84-
91UbiquitinationLTYYCCKKDLCNFNE
CEEEEECHHCCCHHH
41.86-
102GPI-anchorNFNEQLENGGTSLSE
CHHHHHHHCCCCCCH
63.898276756

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CD59_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CD59_HUMAN !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CO9_HUMANC9physical
7523406
GAG_HV1H2gagphysical
10708443
ENV_HV1H2envphysical
10708443

Drug and Disease Associations
Kegg Disease
H00106 Complement regulatory protein defects, including the following six diseases: C1 inhibitor deficiency
OMIM Disease
612300Hemolytic 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.
Regulatory Network of CD59_HUMAN

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Related Literatures of Post-Translational Modification
GPI-anchor
ReferencePubMed
"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
ReferencePubMed
"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
ReferencePubMed
"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.

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