Associated Structures
Accession: P02786 UniProtKB/Swiss-Prot Entry
UniProtKB/Swiss-Prot PTM Description
N- and O-glycosylated, phosphorylated and palmitoylated. The serum form is only glycosylated, Proteolytically cleaved on Arg-100 to produce the soluble serum form (sTfR), Palmitoylated on both Cys-62 and Cys-67. Cys-62 seems to be the major site of palmitoylation
Glycosylation Sites
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-727 | Associated Structures: 7 | global | GlycoSuite |
Position | Structures | Description | Evidence |
---|---|---|---|
THR-104 | Associated Structures: 12 | global | GlycoSuite |
Site-Specific Information
A number of glycan structures have been assigned to specific glycosylation sites
Position | Structures | Description | Evidence |
---|---|---|---|
ASN-727 | Associated Structures: 7 | Site specific | GlycoSuite |
THR-104 | Associated Structures: 4 | Site specific | GlycoSuite |
Notes
Accompanying information sourced from GlycoSuiteDB
- ASN-727 [HAYES ET AL. (1995) GLYCOBIOLOGY 5:227-232
Sequence
Biological Associations
References 5
-
Presence of O-linked oligosaccharide on a threonine residue in the human transferrin receptor.
PubMed: 1421756 Year: 1992
-
PubMed: 7780197 Year: 1995
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Identification of the O-linked glycosylation site of the human transferrin receptor.
PubMed: 1421757 Year: 1992
-
Structure of the N-linked oligosaccharides of the human transferrin receptor.
PubMed: 1555586 Year: 1992
-
Human transferrin receptor contains O-linked oligosaccharides.
PubMed: 2403553 Year: 1990