GLPA_HUMAN - dbPTM
GLPA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLPA_HUMAN
UniProt AC P02724
Protein Name Glycophorin-A
Gene Name GYPA
Organism Homo sapiens (Human).
Sequence Length 150
Subcellular Localization Cell membrane
Single-pass type I membrane protein . Appears to be colocalized with SLC4A1.
Protein Description Glycophorin A is the major intrinsic membrane protein of the erythrocyte. The N-terminal glycosylated segment, which lies outside the erythrocyte membrane, has MN blood group receptors. Appears to be important for the function of SLC4A1 and is required for high activity of SLC4A1. May be involved in translocation of SLC4A1 to the plasma membrane. Is a receptor for influenza virus. Is a receptor for Plasmodium falciparum erythrocyte-binding antigen 175 (EBA-175); binding of EBA-175 is dependent on sialic acid residues of the O-linked glycans. Appears to be a receptor for Hepatitis A virus (HAV)..
Protein Sequence MYGKIIFVLLLSEIVSISASSTTGVAMHTSTSSSVTKSYISSQTNDTHKRDTYAATPRAHEVSEISVRTVYPPEEETGERVQLAHHFSEPEITLIIFGVMAGVIGTILLISYGIRRLIKKSPSDVKPLPSPDTDVPLSSVEIENPETSDQ
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
2Phosphorylation------MYGKIIFVL
------CCHHHHHHH
27.42-
2 (in isoform 3)Phosphorylation-27.4222673903
12 (in isoform 3)Phosphorylation-25.8322673903
14 (in isoform 3)Phosphorylation-2.3722673903
21O-linked_GlycosylationIVSISASSTTGVAMH
HHHCCCCCCCCEEEE
29.708286855
22O-linked_GlycosylationVSISASSTTGVAMHT
HHCCCCCCCCEEEEE
25.698286855
23O-linked_GlycosylationSISASSTTGVAMHTS
HCCCCCCCCEEEEEC
31.448286855
29O-linked_GlycosylationTTGVAMHTSTSSSVT
CCCEEEEECCCCCCC
22.188286855
30O-linked_GlycosylationTGVAMHTSTSSSVTK
CCEEEEECCCCCCCH
16.188286855
31O-linked_GlycosylationGVAMHTSTSSSVTKS
CEEEEECCCCCCCHH
33.518286855
32O-linked_GlycosylationVAMHTSTSSSVTKSY
EEEEECCCCCCCHHH
22.008286855
36O-linked_GlycosylationTSTSSSVTKSYISSQ
ECCCCCCCHHHHHCC
19.0725452425
38O-linked_GlycosylationTSSSVTKSYISSQTN
CCCCCCHHHHHCCCC
20.528286855
41O-linked_GlycosylationSVTKSYISSQTNDTH
CCCHHHHHCCCCCCC
14.258286855
44O-linked_GlycosylationKSYISSQTNDTHKRD
HHHHHCCCCCCCCCC
36.698286855
45N-linked_GlycosylationSYISSQTNDTHKRDT
HHHHCCCCCCCCCCC
44.548286855
52O-linked_GlycosylationNDTHKRDTYAATPRA
CCCCCCCCCCCCCCC
21.068286855
56O-linked_GlycosylationKRDTYAATPRAHEVS
CCCCCCCCCCCEECE
12.728286855
63O-linked_GlycosylationTPRAHEVSEISVRTV
CCCCEECEEEEEEEE
26.658286855
66O-linked_GlycosylationAHEVSEISVRTVYPP
CEECEEEEEEEECCC
11.078286855
69O-linked_GlycosylationVSEISVRTVYPPEEE
CEEEEEEEECCCHHH
23.418286855
121PhosphorylationIRRLIKKSPSDVKPL
HHHHHHCCHHHCCCC
25.3223025827
123PhosphorylationRLIKKSPSDVKPLPS
HHHHCCHHHCCCCCC
63.2328857561
130PhosphorylationSDVKPLPSPDTDVPL
HHCCCCCCCCCCCCC
42.9928192239
133PhosphorylationKPLPSPDTDVPLSSV
CCCCCCCCCCCCHHE
42.1330242111
138PhosphorylationPDTDVPLSSVEIENP
CCCCCCCHHEEECCC
26.6826657352
139PhosphorylationDTDVPLSSVEIENPE
CCCCCCHHEEECCCC
31.3028060719
147PhosphorylationVEIENPETSDQ----
EEECCCCCCCC----
38.5723025827
148PhosphorylationEIENPETSDQ-----
EECCCCCCCC-----
32.147798177

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 GLPA_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLPA_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 GLPA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SGTA_HUMANSGTAphysical
25416956
KEAP1_HUMANKEAP1physical
25416956
ATR_HUMANATRphysical
28514442
CLDN1_HUMANCLDND1physical
28514442
TM192_HUMANTMEM192physical
28514442
GOGA7_HUMANGOLGA7physical
28514442
TCAF2_HUMANFAM115Cphysical
28514442
EF1A2_HUMANEEF1A2physical
28514442
S22AI_HUMANSLC22A18physical
28514442
STAT2_HUMANSTAT2physical
28514442
DYN3_HUMANDNM3physical
28514442

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 GLPA_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.";
Pisano A., Redmond J.W., Williams K.L., Gooley A.A.;
Glycobiology 3:429-435(1993).
Cited for: GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31;SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56;SER-63; SER-66 AND THR-69, AND PARTIAL PROTEIN SEQUENCE.
"Amino-acid sequence and oligosaccharide attachment sites of humanerythrocyte glycophorin.";
Tomita M., Marchesi V.T.;
Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975).
Cited for: PROTEIN SEQUENCE OF 20-150.
O-linked Glycosylation
ReferencePubMed
"Glycosylation sites identified by solid-phase Edman degradation: O-linked glycosylation motifs on human glycophorin A.";
Pisano A., Redmond J.W., Williams K.L., Gooley A.A.;
Glycobiology 3:429-435(1993).
Cited for: GLYCOSYLATION AT SER-21; THR-22; THR-23; THR-29; SER-30; THR-31;SER-32; THR-36; SER-38; SER-41; THR-44; ASN-45; THR-52; THR-56;SER-63; SER-66 AND THR-69, AND PARTIAL PROTEIN SEQUENCE.
"Amino-acid sequence and oligosaccharide attachment sites of humanerythrocyte glycophorin.";
Tomita M., Marchesi V.T.;
Proc. Natl. Acad. Sci. U.S.A. 72:2964-2968(1975).
Cited for: PROTEIN SEQUENCE OF 20-150.

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