GLPC_HUMAN - dbPTM
GLPC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLPC_HUMAN
UniProt AC P04921
Protein Name Glycophorin-C
Gene Name GYPC
Organism Homo sapiens (Human).
Sequence Length 128
Subcellular Localization Cell membrane
Single-pass type III membrane protein. Linked to the membrane via band 4.1.
Protein Description This protein is a minor sialoglycoprotein in human erythrocyte membranes. The blood group Gerbich antigens and receptors for Plasmodium falciparum merozoites are most likely located within the extracellular domain. Glycophorin-C plays an important role in regulating the stability of red cells..
Protein Sequence MWSTRSPNSTAWPLSLEPDPGMASASTTMHTTTIAEPDPGMSGWPDGRMETSTPTIMDIVVIAGVIAAVAIVLVSLLFVMLRYMYRHKGTYHTNEAKGTEFAESADAALQGDPALQDAGDSSRKEYFI
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
3O-linked_Glycosylation-----MWSTRSPNST
-----CCCCCCCCCC		16.797106126
4O-linked_Glycosylation----MWSTRSPNSTA
----CCCCCCCCCCC		21.477106126
6O-linked_Glycosylation--MWSTRSPNSTAWP
--CCCCCCCCCCCCC		28.647106126
6Phosphorylation--MWSTRSPNSTAWP
--CCCCCCCCCCCCC		28.6422210691
8N-linked_GlycosylationMWSTRSPNSTAWPLS
CCCCCCCCCCCCCCC		53.921991173
8N-linked_GlycosylationMWSTRSPNSTAWPLS
CCCCCCCCCCCCCCC		53.921991173
9O-linked_GlycosylationWSTRSPNSTAWPLSL
CCCCCCCCCCCCCCC		23.927106126
10O-linked_GlycosylationSTRSPNSTAWPLSLE
CCCCCCCCCCCCCCC		39.117106126
15O-linked_GlycosylationNSTAWPLSLEPDPGM
CCCCCCCCCCCCCCC		26.977106126
24O-linked_GlycosylationEPDPGMASASTTMHT
CCCCCCCCCCCEEEE		17.547106126
26O-linked_GlycosylationDPGMASASTTMHTTT
CCCCCCCCCEEEEEE		23.167106126
27O-linked_GlycosylationPGMASASTTMHTTTI
CCCCCCCCEEEEEEE		28.057106126
28O-linked_GlycosylationGMASASTTMHTTTIA
CCCCCCCEEEEEEEC		12.407106126
28PhosphorylationGMASASTTMHTTTIA
CCCCCCCEEEEEEEC		12.4022210691
31O-linked_GlycosylationSASTTMHTTTIAEPD
CCCCEEEEEEECCCC		18.147106126
32O-linked_GlycosylationASTTMHTTTIAEPDP
CCCEEEEEEECCCCC		11.097106126
33O-linked_GlycosylationSTTMHTTTIAEPDPG
CCEEEEEEECCCCCC		21.247106126
42O-linked_GlycosylationAEPDPGMSGWPDGRM
CCCCCCCCCCCCCCC		43.5522171320
97UbiquitinationTYHTNEAKGTEFAES
CEECCCCCCCHHHHH		61.25-
99PhosphorylationHTNEAKGTEFAESAD
ECCCCCCCHHHHHHH		27.5028464451
104PhosphorylationKGTEFAESADAALQG
CCCHHHHHHHHHHCC		28.1926657352
121PhosphorylationALQDAGDSSRKEYFI
HHHCCCCCCCCCCCC		30.9928348404
122PhosphorylationLQDAGDSSRKEYFI-
HHCCCCCCCCCCCC-		52.7028348404
126PhosphorylationGDSSRKEYFI-----
CCCCCCCCCC-----		15.0328450419
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 GLPC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLPC_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 GLPC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GLPC_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLPC_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C)from human erythrocyte membranes.";
Dahr W., Beyreuther K., Kordowicz M., Krueger J.;
Eur. J. Biochem. 125:57-62(1982).
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-48, AND GLYCOSYLATION AT SER-3;THR-4; SER-6; ASN-8; SER-9; THR-10; SER-15; SER-24; SER-26; THR-27;THR-28; THR-31; THR-32; THR-33 AND SER-42.
O-linked Glycosylation
ReferencePubMed
"Human urinary glycoproteomics; attachment site specific analysis ofN-and O-linked glycosylations by CID and ECD.";
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
Mol. Cell. Proteomics 0:0-0(2011).
Cited for: GLYCOSYLATION AT SER-42, STRUCTURE OF CARBOHYDRATES, AND MASSSPECTROMETRY.
"N-terminal amino acid sequence of sialoglycoprotein D (glycophorin C)from human erythrocyte membranes.";
Dahr W., Beyreuther K., Kordowicz M., Krueger J.;
Eur. J. Biochem. 125:57-62(1982).
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-48, AND GLYCOSYLATION AT SER-3;THR-4; SER-6; ASN-8; SER-9; THR-10; SER-15; SER-24; SER-26; THR-27;THR-28; THR-31; THR-32; THR-33 AND SER-42.
"Glycophorins B and C from human erythrocyte membranes. Purificationand sequence analysis.";
Blanchard D., Dahr W., Hummel M., Latron F., Beyreuther K.,Cartron J.-P.;
J. Biol. Chem. 262:5808-5811(1987).
Cited for: PROTEIN SEQUENCE OF 49-88.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-104, AND MASSSPECTROMETRY.

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