UniProt ID | ASGR2_HUMAN | |
---|---|---|
UniProt AC | P07307 | |
Protein Name | Asialoglycoprotein receptor 2 | |
Gene Name | ASGR2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 311 | |
Subcellular Localization |
Membrane Single-pass type II membrane protein. |
|
Protein Description | Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transported to a sorting organelle, where receptor and ligand are disassociated. The receptor then returns to the cell membrane surface.. | |
Protein Sequence | MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFSLLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGSVGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVNWVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDSDGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVCEKRRNATGEVA | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
12 | Phosphorylation | FQDIQQLSSEENDHP HHHHHHHCCCCCCCC | 31.22 | 1924301 | |
13 | Phosphorylation | QDIQQLSSEENDHPF HHHHHHCCCCCCCCC | 58.48 | 26422651 | |
54 | S-palmitoylation | QPLAQRLCSMVCFSL HHHHHHHHHHHHHHH | 2.41 | - | |
102 | N-linked_Glycosylation | SLKEAFSNFSSSTLT HHHHHHHCCCCCCCE | 34.07 | 16335952 | |
134 | Acetylation | SLGAKLEKQQQDLKA HHHHHHHHHHHHHHC | 64.94 | 23749302 | |
170 | N-linked_Glycosylation | QMELLHSNGSQRTCC HHHHHHCCCCCCEEE | 43.30 | 19159218 | |
305 | N-linked_Glycosylation | WVCEKRRNATGEVA- HHHHHHHCCCCCCC- | 45.98 | UniProtKB CARBOHYD |
Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
---|---|---|---|---|---|---|
12 | S | Phosphorylation | Kinase | PKC-FAMILY | - | GPS |
12 | S | Phosphorylation | Kinase | PKC_GROUP | - | PhosphoELM |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ASGR2_HUMAN !! |
* 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 ASGR2_HUMAN !! |
Kegg Disease | ||||||
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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. |
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N-linked Glycosylation | |
Reference | PubMed |
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry."; Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; J. Proteome Res. 8:651-661(2009). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102 AND ASN-170, AND MASSSPECTROMETRY. | |
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,hydrazide chemistry, and mass spectrometry."; Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,Moore R.J., Smith R.D.; J. Proteome Res. 4:2070-2080(2005). Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-102, AND MASSSPECTROMETRY. |