Search Results
Overview
| Uniprot ID | P60468 |
|---|---|
| Protein Name | Protein transport protein Sec61 subunit beta |
| Gene Name | SEC61B |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 20 | SSGRSPSKAVAARAA |
| 35 | GSTVRQRKNASCGTR |
Function
Component of SEC61 channel-forming translocon complex that mediates transport of signal peptide-containing precursor polypeptides across the endoplasmic reticulum (ER) (PubMed:12475939). Forms a ribosome receptor and a gated pore in the ER membrane, both functions required for cotranslational translocation of nascent polypeptides (PubMed:12475939). The SEC61 channel is also involved in ER membrane insertion of transmembrane proteins: it mediates membrane insertion of the first few transmembrane segments of proteins, while insertion of subsequent transmembrane regions of multi-pass membrane proteins is mediated by the multi-pass translocon (MPT) complex (PubMed:32820719, PubMed:36261522). The SEC61 channel cooperates with the translocating protein TRAM1 to import nascent proteins into the ER (PubMed:19121997)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0044322 | endoplasmic reticulum quality control compartment |
| Cellular Component | GO:0031205 | endoplasmic reticulum Sec complex |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005784 | Sec61 translocon complex |
| Molecular Function | GO:0048408 | epidermal growth factor binding |
| Molecular Function | GO:0005085 | guanyl-nucleotide exchange factor activity |
| Molecular Function | GO:0043022 | ribosome binding |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0036503 | ERAD pathway |
| Biological Process | GO:0031204 | post-translational protein targeting to membrane, translocation |
| Biological Process | GO:0030970 | retrograde protein transport, ER to cytosol |
| Biological Process | GO:0006616 | SRP-dependent cotranslational protein targeting to membrane, translocation |
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] 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] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[4] Bao Q, Wan N, He Z, Cao J, Yuan W et al.. Subcellular Proteomic Mapping of Lysine Lactylation.. J Am Soc Mass Spectrom 35(12):3221-3232. 2024 Dec 4. PMID: 39569522.
[5] 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.