Search Results
Overview
| Uniprot ID | O94905 |
|---|---|
| Protein Name | Erlin-2 |
| Gene Name | ERLIN2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 192 | LMESEKTKLLIAAQK |
| 199 | KLLIAAQKQKVVEKE |
| 205 | QKQKVVEKEAETERK |
| 236 | YGQKVMEKETEKKIS |
| 241 | MEKETEKKISEIEDA |
| 275 | IAEANKLKLTPEYLQ |
| 287 | YLQLMKYKAIASNSK |
Function
Component of the ERLIN1/ERLIN2 complex which mediates the endoplasmic reticulum-associated degradation (ERAD) of inositol 1,4,5-trisphosphate receptors (IP3Rs) such as ITPR1 (PubMed:17502376, PubMed:19240031). Promotes sterol-accelerated ERAD of HMGCR probably implicating an AMFR/gp78-containing ubiquitin ligase complex (PubMed:21343306). Involved in regulation of cellular cholesterol homeostasis by regulation the SREBP signaling pathway. May promote ER retention of the SCAP-SREBF complex (PubMed:24217618)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0045121 | membrane raft |
| Cellular Component | GO:0005886 | plasma membrane |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0015485 | cholesterol binding |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0008203 | cholesterol metabolic process |
| Biological Process | GO:0036503 | ERAD pathway |
| Biological Process | GO:0045541 | negative regulation of cholesterol biosynthetic process |
| Biological Process | GO:0045717 | negative regulation of fatty acid biosynthetic process |
| Biological Process | GO:0045540 | regulation of cholesterol biosynthetic process |
| Biological Process | GO:0032933 | SREBP signaling pathway |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Yan M, Tu H, Tang S, Gai Z, Shi Q et al.. Lactylated Proteomic Analysis Reveals Functional Implications of Lysine Lactylation In Asthenozoospermia.. Mol Cell Proteomics 24(12):101439. 2025 Dec. PMID: 41192556.