Search Results
Overview
| Uniprot ID | Q9P2E9 |
|---|---|
| Protein Name | Ribosome-binding protein 1 |
| Gene Name | RRBP1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1014 | REAVEQQKVKNNDLR |
| 1026 | DLREKNWKAMEALAT |
| 1039 | ATAEQACKEKLLSLT |
| 1098 | EKGPTLLKHPPAPAE |
| 1159 | EEQVWRAKVGAAEEE |
| 1169 | AAEEELQKSRVTVKH |
| 1175 | QKSRVTVKHLEEIVE |
| 1185 | EEIVEKLKGELESSD |
| 1221 | AECQNYAKEVAGLRQ |
| 1241 | QSQLDAAKSEAQKQS |
| 1246 | AAKSEAQKQSDELAL |
| 1310 | DEQTQRQKLTAEFEE |
| 1358 | ERLEKEKKLTSDLGR |
| 200 | ATGTTQGKKAEGTQN |
| 211 | GTQNQSKKAEGAPNQ |
| 221 | GAPNQGRKAEGTPNQ |
| 230 | EGTPNQGKKTEGTPN |
| 240 | EGTPNQGKKAEGTPN |
| 261 | GTPNQGKKAEGAQNQ |
| 270 | EGAQNQGKKVDTTPN |
| 281 | TTPNQGKKVEGAPTQ |
| 291 | GAPTQGRKAEGAQNQ |
| 310 | EGAQNQGKKAEGAQN |
| 330 | EGAQNQGKKAEGAQN |
| 501 | GAQNQGKKAEGAQNQ |
| 511 | GAQNQGQKGEGAQNQ |
| 521 | GAQNQGKKTEGAQGK |
| 538 | ERSPNQGKKGEGAPI |
| 548 | EGAPIQGKKADSVAN |
| 559 | SVANQGTKVEGITNQ |
| 568 | EGITNQGKKAEGSPS |
| 569 | GITNQGKKAEGSPSE |
| 589 | GSPNQGKKADAAANQ |
| 599 | AAANQGKKTESASVQ |
| 620 | AQSPEAPKQEAPAKK |
| 634 | KKSGSKKKGEPGPPD |
| 677 | LIEILSEKAGIIQDT |
| 691 | TWHKATQKGDPVAIL |
| 699 | GDPVAILKRQLEEKE |
| 707 | RQLEEKEKLLATEQE |
| 720 | QEDAAVAKSKLRELN |
| 722 | DAAVAKSKLRELNKE |
| 728 | SKLRELNKEMAAEKA |
| 736 | EMAAEKAKAAAGEAK |
| 771 | ASYREHVKEVQQLQG |
| 779 | EVQQLQGKIRTLQEQ |
| 819 | ATSQVESKQNAELAK |
| 841 | VSKELVEKSEAVRQD |
| 858 | QRKALEAKAAAFEKQ |
| 864 | AKAAAFEKQVLQLQA |
| 882 | ESEEALQKRLDEVSR |
| 932 | SEAEVRSKCEELSGL |
| 990 | DQQQTRLKELESQVS |
Function
Acts as a ribosome receptor and mediates interaction between the ribosome and the endoplasmic reticulum membrane
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0005789 | endoplasmic reticulum membrane |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0005840 | ribosome |
| Molecular Function | GO:0003723 | RNA binding |
| Molecular Function | GO:0038023 | signaling receptor activity |
| Biological Process | GO:0001649 | osteoblast differentiation |
| Biological Process | GO:0015031 | protein transport |
| Biological Process | GO:0006412 | translation |
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] Yang YH, Wang QC, Kong J, Yang JT, Liu JF. Global profiling of lysine lactylation in human lungs.. Proteomics 23(15):e2200437. 2023 Aug. PMID: 37170646.
[4] 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.
[5] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[6] 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.