Search Results
Overview
| Uniprot ID | Q96EV2 |
|---|---|
| Protein Name | RNA-binding protein 33 |
| Gene Name | RBM33 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 1061 | IQGIHPAKKAIMHGR |
| 1062 | QGIHPAKKAIMHGRG |
| 1085 | RGRLMPNKQNLRVVE |
| 692 | TTSQNVSKRPMQQMQ |
| 798 | RLKIEEQKRLREEIL |
| 877 | VKNRLLVKNQDVSIS |
| 908 | QYQGQQMKALKHLRQ |
| 929 | SQTQPLHKVLPIKPA |
| 984 | DGPHISSKVRVIKLS |
| 989 | SSKVRVIKLSGGGGE |
Function
RNA reader protein, which recognizes and binds specific RNAs, thereby regulating RNA metabolic processes, such as mRNA export, mRNA stability and/or translation (PubMed:35589130, PubMed:37257451). Binds a subset of intronless RNAs containing GC-rich elements, such as NORAD, and promotes their nuclear export by recruiting target RNAs to components of the NXF1-NXT1 RNA export machinery (PubMed:35589130). Specifically recognizes and binds N6-methyladenosine (m6A)-containing mRNAs, promoting their demethylation by ALKBH5 (PubMed:37257451). Acts as an molecular adapter, which (1) promotes ALKBH5 recruitment to m6A-containing transcripts and (2) activates ALKBH5 demethylase activity by recruiting SENP1, leading to ALKBH5 deSUMOylation and subsequent activation (PubMed:37257451)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:1990247 | N6-methyladenosine-containing RNA reader activity |
| Molecular Function | GO:0030674 | protein-macromolecule adaptor activity |
| Molecular Function | GO:0003723 | RNA binding |
| Biological Process | GO:0051028 | mRNA transport |
| Biological Process | GO:0043488 | regulation of mRNA stability |
| Biological Process | GO:0006405 | RNA export from nucleus |
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] 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.
[3] 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.
[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.