Overview
| Uniprot ID | Q9Y265 |
|---|
| Protein Name | RuvB-like 1 |
|---|
| Gene Name | RUVBL1 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 171 |
AKGTKQLKLDPSIFE |
Function
Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') activity; hexamerization is thought to be critical for ATP hydrolysis and adjacent subunits in the ring-like structure contribute to the ATPase activity (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. 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). Essential for cell proliferation (PubMed:14506706). May be able to bind plasminogen at cell surface and enhance plasminogen activation (PubMed:11027681)
Protein Sequence
10
MKIEEVKSTT
20
KTQRIASHSH
30
VKGLGLDESG
40
LAKQAASGLV
50
GQENAREACG
60
VIVELIKSKK
70
MAGRAVLLAG
80
PPGTGKTALA
90
LAIAQELGSK
100
VPFCPMVGSE
110
VYSTEIKKTE
120
VLMENFRRAI
130
GLRIKETKEV
140
YEGEVTELTP
150
CETENPMGGY
160
GKTISHVIIG
170
LKTAKGTKQL
180
KLDPSIFESL
190
QKERVEAGDV
200
IYIEANSGAV
210
KRQGRCDTYA
220
TEFDLEAEEY
230
VPLPKGDVHK
240
KKEIIQDVTL
250
HDLDVANARP
260
QGGQDILSMM
270
GQLMKPKKTE
280
ITDKLRGEIN
290
KVVNKYIDQG
300
IAELVPGVLF
310
VDEVHMLDIE
320
CFTYLHRALE
330
SSIAPIVIFA
340
SNRGNCVIRG
350
TEDITSPHGI
360
PLDLLDRVMI
370
IRTMLYTPQE
380
MKQIIKIRAQ
390
TEGINISEEA
400
LNHLGEIGTK
410
TTLRYSVQLL
420
TPANLLAKIN
430
GKDSIEKEHV
440
EEISELFYDA
450
KSSAKILADQ
QDKYMK
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005813 |
centrosome |
| Cellular Component |
GO:0036064 |
ciliary basal body |
| Cellular Component |
GO:0005829 |
cytosol |
| Cellular Component |
GO:0120293 |
dynein axonemal particle |
| 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:0016607 |
nuclear speck |
| 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:0045296 |
cadherin binding |
| Molecular Function |
GO:0003678 |
DNA helicase activity |
| Molecular Function |
GO:0017025 |
TBP-class protein binding |
| Molecular Function |
GO:0001094 |
TFIID-class transcription factor complex binding |
| Molecular Function |
GO:0003713 |
transcription coactivator activity |
| Biological Process |
GO:0000492 |
box C/D snoRNP assembly |
| Biological Process |
GO:0051301 |
cell division |
| 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:0090263 |
positive 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: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:0007283 |
spermatogenesis |
| Biological Process |
GO:0090671 |
telomerase RNA localization to Cajal body |
| Biological Process |
GO:0000723 |
telomere maintenance |
Reference
[1] 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.