RUVBL1
entrez
8607
canonical
uniprot
Q9Y265
canonical
ensembl
ENSG00000175792
resolver
ensp
ENSP00000318297
resolver
ensp
ENSP00000420738
resolver
ensp
ENSP00000668472
resolver
ensp
ENSP00000668477
resolver
ensp
ENSP00000708368
resolver
ensp
ENSP00000708371
resolver
enst
ENST00000464873
resolver
genesymbol
RUVBL1
resolver
genesymbol_syn
INO80H
resolver
genesymbol_syn
NMP238
resolver
genesymbol_syn
TIP49
resolver
genesymbol_syn
TIP49A
resolver
hgnc
HGNC:10474
resolver
uniprot
A0A384MTR5
resolver
uniprot
B2R5S0
resolver
uniprot
B3KRS7
resolver
uniprot
E7ETR0
resolver
uniprot
P82276
resolver
uniprot
Q1KMR0
resolver
uniprot
Q53HK5
resolver
uniprot
Q53HL7
resolver
uniprot
Q53Y27
resolver
uniprot
Q9BSX9
resolver
uniprot_entry
A0A384MTR5_HUMAN
resolver
uniprot_entry
B3KRS7_HUMAN
resolver
uniprot_entry
E7ETR0_HUMAN
resolver
uniprot_entry
RUVB1_HUMAN
resolver
uniprot_sec
B2R5S0
resolver
uniprot_sec
P82276
resolver
uniprot_sec
Q1KMR0
resolver
uniprot_sec
Q53HK5
resolver
uniprot_sec
Q53HL7
resolver
uniprot_sec
Q53Y27
resolver
uniprot_sec
Q9BSX9
resolver
amino_acid_sequence
MKIEEVKSTTKTQRIASHSHVKGLGLDESGLAKQAASGLVGQENAREACGVIVELIKSKKMAGRAVLLAGPPGTGKTALALAIAQELGSKVPFCPMVGSEVYSTEIKKTEVLMENFRRAIGLRIKETKEVYEGEVTELTPCETENPMGGYGKTISHVIIGLKTAKGTKQLKLDPSIFESLQKERVEAGDVIYIEANSGAVKRQGRCDTYATEFDLEAEEYVPLPKGDVHKKKEIIQDVTLHDLDVANARPQGGQDILSMMGQLMKPKKTEITDKLRGEINKVVNKYIDQGIAELVPGVLFVDEVHMLDIECFTYLHRALESSIAPIVIFASNRGNCVIRGTEDITSPHGIPLDLLDRVMIIRTMLYTPQEMKQIIKIRAQTEGINISEEALNHLGEIGTKTTLRYSVQLLTPANLLAKINGKDSIEKEHVEEISELFYDAKSSAKILADQQDKYMK
uniprot
proteins
ec_number
3.6.4.12
uniprot
proteins
function
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}.
uniprot
proteins
mass_dalton
50228
uniprot
proteins
mutagenesis
MUTAGEN 76; /note="K->M: No effect on interaction with NOPCHAP1."; /evidence="ECO:0000269|PubMed:33367824"; MUTAGEN 302; /note="D->N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation."; /evidence="ECO:0000269|PubMed:10882073, ECO:0000269|PubMed:14695187, ECO:0000269|PubMed:17060327, ECO:0000269|PubMed:17157868"; MUTAGEN 303; /note="E->Q: Reduces ATPase activity. Decreases interaction with NOPCHAP1. No effect on formation of RUVBL1-RUVBL2 heteromeric complex."; /evidence="ECO:0000269|PubMed:33205750, ECO:0000269|PubMed:33367824
uniprot
proteins
protein_family
RuvB family
uniprot
proteins
pubmed
10428817
uniprot
proteins
pubmed
10524211
uniprot
proteins
pubmed
10882073
uniprot
proteins
pubmed
10966108
uniprot
proteins
pubmed
11027681
uniprot
proteins
pubmed
11080158
uniprot
proteins
pubmed
11839798
uniprot
proteins
pubmed
12963728
uniprot
proteins
pubmed
14506706
uniprot
proteins
pubmed
14695187
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14966270
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16014379
uniprot
proteins
pubmed
16230350
uniprot
proteins
pubmed
17060327
uniprot
proteins
pubmed
17157868
uniprot
proteins
pubmed
17636026
uniprot
proteins
pubmed
17761535
uniprot
proteins
pubmed
17967892
uniprot
proteins
pubmed
18026119
uniprot
proteins
pubmed
19054851
uniprot
proteins
pubmed
19299493
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
20864032
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21303910
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23824326
uniprot
proteins
pubmed
24463511
uniprot
proteins
pubmed
25114211
uniprot
proteins
pubmed
25218447
uniprot
proteins
pubmed
25437307
uniprot
proteins
pubmed
25755297
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26812014
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28561026
uniprot
proteins
pubmed
30337683
uniprot
proteins
pubmed
31121004
uniprot
proteins
pubmed
31738558
uniprot
proteins
pubmed
33205750
uniprot
proteins
pubmed
33367824
uniprot
proteins
pubmed
36161484
uniprot
proteins
pubmed
9588198
uniprot
proteins
pubmed
9774387
uniprot
proteins
pubmed
9813143
uniprot
proteins
pubmed
9843967
uniprot
proteins
sequence_length
456
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm {ECO:0000269|PubMed:11027681}. Membrane {ECO:0000269|PubMed:11027681}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE26}. Note=Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in the cytoplasm and associated with the cell membranes. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells.
uniprot
proteins