Search Results
Overview
| Uniprot ID | P07307 |
|---|---|
| Protein Name | Asialoglycoprotein receptor 2 |
| Gene Name | ASGR2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 134 | SLGAKLEKQQQDLKA |
Function
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
10
MAKDFQDIQQ
20
LSSEENDHPF
30
HQGEGPGTRR
40
LNPRRGNPFL
50
KGPPPAQPLA
60
QRLCSMVCFS
70
LLALSFNILL
80
LVVICVTGSQ
90
SEGHGGAQLQ
100
AELRSLKEAF
110
SNFSSSTLTE
120
VQAISTHGGS
130
VGDKITSLGA
140
KLEKQQQDLK
150
ADHDALLFHL
160
KHFPVDLRFV
170
ACQMELLHSN
180
GSQRTCCPVN
190
WVEHQGSCYW
200
FSHSGKAWAE
210
AEKYCQLENA
220
HLVVINSWEE
230
QKFIVQHTNP
240
FNTWIGLTDS
250
DGSWKWVDGT
260
DYRHNYKNWA
270
VTQPDNWHGH
280
ELGGSEDCVE
290
VQPDGRWNDD
300
FCLQVYRWVC
310
EKRRNATGEV
A
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0044322 | endoplasmic reticulum quality control compartment |
| Cellular Component | GO:0009897 | external side of plasma membrane |
| Cellular Component | GO:0048471 | perinuclear region of cytoplasm |
| Cellular Component | GO:0005886 | plasma membrane |
| Molecular Function | GO:0004873 | asialoglycoprotein receptor activity |
| Molecular Function | GO:0005537 | D-mannose binding |
| Molecular Function | GO:0042806 | fucose binding |
| Molecular Function | GO:0038187 | pattern recognition receptor activity |
| Biological Process | GO:0007166 | cell surface receptor signaling pathway |
| Biological Process | GO:0006897 | endocytosis |
| Biological Process | GO:0006955 | immune response |
Reference
[1] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.