dbPTM

CD59_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
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

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
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

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
CO9_HUMAN	C9	physical	7523406
GAG_HV1H2	gag	physical	10708443
ENV_HV1H2	env	physical	10708443

Drug and Disease Associations

Kegg Disease
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.

Regulatory Network of CD59_HUMAN

Related Literatures of Post-Translational Modification

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.	17566972 [Abstract]
"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.	16602701 [Abstract]
"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.	14517339 [Abstract]
"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.	9054419 [Abstract]
"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.	8276756 [Abstract]
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.	10805801 [Abstract]
"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.	18780401 [Abstract]
"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.	8670172 [Abstract]
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.	19534553 [Abstract]