RUVBL1
UniProt ID: Q9Y265
Entrez ID: 8607
Protein name: RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (54 kDa erythrocyte cytosolic protein) (ECP-54) (INO80 complex subunit H) (Nuclear matrix protein 238) (NMP 238) (Pontin 52) (TIP49a) (TIP60-associated protein 54-alpha) (TAP54-alpha)
External links: UniprotKB HGNC RefSeq COSMIC
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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 o...
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). {ECO:0000269|PubMed:10882073, ECO:0000269|PubMed:11027681, ECO:0000269|PubMed:14506706, ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:17157868, ECO:0000269|PubMed:21303910, ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:33205750}.
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GO - Biological processes (BP):
box C/D snoRNP assembly [GO:0000492]; cell cycle [GO:0007049]; cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; histone acetylation [GO:0016573]; histone exchange [GO:0043486]; histone H2A acetylation [GO:0043968]; histone H4 ace...
box C/D snoRNP assembly [GO:0000492]; cell cycle [GO:0007049]; cell division [GO:0051301]; chromatin remodeling [GO:0006338]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; histone acetylation [GO:0016573]; histone exchange [GO:0043486]; histone H2A acetylation [GO:0043968]; histone H4 acetylation [GO:0043967]; nucleosome mobilization [GO:0042766]; positive regulation of canonical Wnt signaling pathway [GO:0090263]; positive regulation of double-strand break repair via homologous recombination [GO:1905168]; positive regulation of telomerase RNA localization to Cajal body [GO:1904874]; positive regulation of telomere maintenance in response to DNA damage [GO:1904507]; positive regulation of transcription, DNA-templated [GO:0045893]; protein stabilization [GO:0050821]; regulation of apoptotic process [GO:0042981]; regulation of cell cycle [GO:0051726]; regulation of chromosome organization [GO:0033044]; regulation of DNA replication [GO:0006275]; regulation of DNA strand elongation [GO:0060382]; regulation of double-strand break repair [GO:2000779]; regulation of embryonic development [GO:0045995]; regulation of growth [GO:0040008]; regulation of transcription, DNA-templated [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357]; spermatogenesis [GO:0007283]; telomere maintenance [GO:0000723]
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GO - Molecular function (MF):
ADP binding [GO:0043531]; ATPase binding [GO:0051117]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; DNA helicase activity [GO:0003678]; TBP-class protein binding [GO:0017025]; TFIID-class transcription factor complex binding [GO:0001094]; transcripti...
ADP binding [GO:0043531]; ATPase binding [GO:0051117]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; DNA helicase activity [GO:0003678]; TBP-class protein binding [GO:0017025]; TFIID-class transcription factor complex binding [GO:0001094]; transcription coactivator activity [GO:0003713]
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GO - Cellular component (CC):
chaperone complex [GO:0101031]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular exosome [GO:0070062]; Ino80 complex [GO:0031011]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; MLL1 complex [GO:0071339]; NuA4 histone acetyltransferase complex [GO:003526...
chaperone complex [GO:0101031]; cytosol [GO:0005829]; dynein axonemal particle [GO:0120293]; extracellular exosome [GO:0070062]; Ino80 complex [GO:0031011]; membrane [GO:0016020]; microtubule organizing center [GO:0005815]; MLL1 complex [GO:0071339]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; R2TP complex [GO:0097255]; ribonucleoprotein complex [GO:1990904]; RPAP3/R2TP/prefoldin-like complex [GO:1990062]; Swr1 complex [GO:0000812]
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RUVBL1
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Kaplan plot for RUVBL1 in
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*NOTE: the Kaplan plots were collected from OncoLnc