Search Results
Overview
| Uniprot ID | Q9Y230 |
|---|---|
| Protein Name | RuvB-like 2 |
| Gene Name | RUVBL2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 365 | STTPYSEKDTKQILR |
| 9 | ATVTATTKVPEIRDV |
Function
Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity (PubMed:10428817, PubMed:17157868, PubMed:33205750). Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A (PubMed:14966270). This modification may both alter nucleosome -DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription (PubMed:14966270). This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair (PubMed:14966270). The NuA4 complex ATPase and helicase activities seem to be, at least in part, contributed by the association of RUVBL1 and RUVBL2 with EP400 (PubMed:14966270). NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage (PubMed:14966270). Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Proposed core component of the chromatin remodeling INO80 complex which exhibits DNA- and nucleosome-activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (PubMed:16230350, PubMed:21303910). Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex (PubMed:10882073, PubMed:16014379). May also inhibit the transcriptional activity of ATF2 (PubMed:11713276). Involved in the endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes (PubMed:25652260). May play a role in regulating the composition of the U5 snRNP complex (PubMed:28561026)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0120293 | dynein axonemal particle |
| Cellular Component | GO:0000791 | euchromatin |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0031011 | Ino80 complex |
| Cellular Component | GO:0016020 | membrane |
| Cellular Component | GO:0071339 | MLL1 complex |
| Cellular Component | GO:0035267 | NuA4 histone acetyltransferase complex |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0101031 | protein folding chaperone complex |
| Cellular Component | GO:0097255 | R2TP complex |
| Cellular Component | GO:1990904 | ribonucleoprotein complex |
| Cellular Component | GO:1990062 | RPAP3/R2TP/prefoldin-like complex |
| Cellular Component | GO:0000812 | Swr1 complex |
| Molecular Function | GO:0043531 | ADP binding |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0016887 | ATP hydrolysis activity |
| Molecular Function | GO:0051117 | ATPase binding |
| Molecular Function | GO:0008013 | beta-catenin binding |
| Molecular Function | GO:0031490 | chromatin DNA binding |
| Molecular Function | GO:0003678 | DNA helicase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0140585 | promoter-enhancer loop anchoring activity |
| Molecular Function | GO:0042803 | protein homodimerization activity |
| Molecular Function | GO:0000978 | RNA polymerase II cis-regulatory region sequence-specific DNA binding |
| Molecular Function | GO:0000979 | RNA polymerase II core promoter sequence-specific DNA binding |
| Molecular Function | GO:0017025 | TBP-class protein binding |
| Molecular Function | GO:0001094 | TFIID-class transcription factor complex binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0000492 | box C/D snoRNP assembly |
| Biological Process | GO:0071392 | cellular response to estradiol stimulus |
| Biological Process | GO:0034644 | cellular response to UV |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0006310 | DNA recombination |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006351 | DNA-templated transcription |
| Biological Process | GO:0071169 | establishment of protein localization to chromatin |
| Biological Process | GO:0090090 | negative regulation of canonical Wnt signaling pathway |
| Biological Process | GO:0045893 | positive regulation of DNA-templated transcription |
| Biological Process | GO:1905168 | positive regulation of double-strand break repair via homologous recombination |
| Biological Process | GO:1904507 | positive regulation of telomere maintenance in response to DNA damage |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0050821 | protein stabilization |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0033044 | regulation of chromosome organization |
| Biological Process | GO:0006275 | regulation of DNA replication |
| Biological Process | GO:0060382 | regulation of DNA strand elongation |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:2000779 | regulation of double-strand break repair |
| Biological Process | GO:0045995 | regulation of embryonic development |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0090671 | telomerase RNA localization to Cajal body |
| Biological Process | GO:0000723 | telomere maintenance |
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] 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.
[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] 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.