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Details on Person UniProt:P98155-1 VLDLR
| Class:Id | ReferenceIsoform:404977 |
|---|---|
| _chainChangeLog | signal peptide:1-27 added on Fri February 6 2015;chain:28-873 added on Fri February 6 2015 |
| _displayName | UniProt:P98155-1 VLDLR |
| _timestamp | 2025-08-15 22:12:55 |
| chain | signal peptide:1-27 chain:28-873 |
| checksum | 8BAC29438A78C2B8 |
| comment | FUNCTION Multifunctional cell surface receptor that binds VLDL and transports it into cells by endocytosis and therefore plays an important role in energy metabolism. Also binds to a wide range of other molecules including Reelin/RELN or apolipoprotein E/APOE-containing ligands as well as clusterin/CLU (PubMed:24381170, PubMed:30873003). In the off-state of the pathway, forms homooligomers or heterooligomers with LRP8 (PubMed:30873003). Upon binding to ligands, homooligomers are rearranged to higher order receptor clusters that transmit the extracellular RELN signal to intracellular signaling processes by binding to DAB1 (PubMed:30873003). This interaction results in phosphorylation of DAB1 leading to the ultimate cell responses required for the correct positioning of newly generated neurons. Later, mediates a stop signal for migrating neurons, preventing them from entering the marginal zone (By similarity).FUNCTION (Microbial infection) Acts as a receptor for Semliki Forest virus.SUBUNIT Homooligomer (PubMed:30873003). Binds to the extracellular matrix protein Reelin/RELN (PubMed:30873003). Interacts with LRP8 (PubMed:30873003). Interacts with LDLRAP1 (By similarity). Interacts with SNX17 (By similarity). Interacts with DAB1. Interacts with PCSK9. Interacts with PAFAH1B3 and PAFAH1B2, the catalytic complex of (PAF-AH (I)) heterotetrameric enzyme; these interactions may modulate the Reelin pathway (PubMed:17330141). Interacts with STX5; this interaction mediates VLDLR translocation from the endoplasmic reticulum to the plasma membrane (PubMed:23701949). Interacts with CLU (PubMed:24381170).SUBUNIT (Microbial infection) Interacts with protein VP1 of the minor-group human rhinoviruses (HRVs) through the second and third LDL-receptor class A domains.SUBUNIT (Microbial infection) Interacts (via class A repeats) with Semliki Forest virus spike glycoprotein E1 (via DIII); this interaction mediates viral entry into host cell.SUBUNIT (Microbial infection) Interacts (via class A repeats) with Eastern equine encephalitis virus spike glycoprotein E2 (via E2-A); this interaction mediates viral entry into host cell.INTERACTION Abundant in heart and skeletal muscle; also ovary and kidney; not in liver.PTM Ubiquitinated at Lys-839 by MYLIP leading to degradation.PTM Glycosylated.DISEASE The disease is caused by variants affecting the gene represented in this entry. |
| created | [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 |
| description | recommendedName: Very low-density lipoprotein receptor shortName: VLDL receptor shortName: VLDL-R |
| geneName | VLDLR |
| identifier | P98155 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Cell membrane Cholesterol metabolism Coated pit Disulfide bond EGF-like domain Endocytosis Glycoprotein Host-virus interaction Intellectual disability Isopeptide bond Lipid metabolism Lipid transport Membrane Proteomics identification Receptor Reference proteome Repeat Signal Steroid metabolism Sterol metabolism Transmembrane Transmembrane helix Transport Ubl conjugation VLDL |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9948485] Weiser, Joel, 2025-05-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | VLDLR |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8995782] ENSEMBL:ENSG00000147852 VLDLR [Homo sapiens] |
| secondaryIdentifier | VLDLR_HUMAN B2RMZ7 D3DRH6 Q5VVF6 |
| sequenceLength | 873 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | P98155-1 |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:P98155-1 VLDLR (404977)
