Search Results
Overview
| Uniprot ID | P08240 |
|---|---|
| Protein Name | Signal recognition particle receptor subunit alpha |
| Gene Name | SRPRA |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 138 | RAPTTMKKFEDSEKA |
| 174 | SKKKGAKKEGSDGPL |
| 220 | KREEFIQKHGRGMEK |
| 233 | EKSNKSTKSDAPKEK |
Function
Component of the signal recognition particle (SRP) complex receptor (SR) (PubMed:16439358). Ensures, in conjunction with the SRP complex, the correct targeting of the nascent secretory proteins to the endoplasmic reticulum membrane system (PubMed:16675701, PubMed:34020957). Forms a guanosine 5'-triphosphate (GTP)-dependent complex with the SRP subunit SRP54 (PubMed:34020957). SRP receptor compaction and GTPase rearrangement drive SRP-mediated cotranslational protein translocation into the ER (PubMed:34020957)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005785 | signal recognition particle receptor complex |
| Molecular Function | GO:0005525 | GTP binding |
| Molecular Function | GO:0003924 | GTPase activity |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0005047 | signal recognition particle binding |
| Biological Process | GO:0006613 | cotranslational protein targeting to membrane |
| Biological Process | GO:0006886 | intracellular protein transport |
| Biological Process | GO:0045047 | protein targeting to ER |
| Biological Process | GO:0006617 | SRP-dependent cotranslational protein targeting to membrane, signal sequence recognition |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] 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.
[3] 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.
[4] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.