RUVBL2
entrez
10856
canonical
uniprot
Q9Y230
canonical
ensembl
ENSG00000183207
resolver
ensp
ENSP00000471524
resolver
ensp
ENSP00000473172
resolver
ensp
ENSP00000486242
resolver
genesymbol
RUVBL2
resolver
genesymbol_syn
INO80J
resolver
genesymbol_syn
TIP48
resolver
genesymbol_syn
TIP49B
resolver
hgnc
HGNC:10475
resolver
uniprot
B3KNL2
resolver
uniprot
B3KQ59
resolver
uniprot
E7ETE5
resolver
uniprot
Q6FIB9
resolver
uniprot
Q6PK27
resolver
uniprot
Q9Y361
resolver
uniprot_entry
B3KNL2_HUMAN
resolver
uniprot_entry
RUVB2_HUMAN
resolver
uniprot_sec
B3KQ59
resolver
uniprot_sec
E7ETE5
resolver
uniprot_sec
Q6FIB9
resolver
uniprot_sec
Q6PK27
resolver
uniprot_sec
Q9Y361
resolver
amino_acid_sequence
MATVTATTKVPEIRDVTRIERIGAHSHIRGLGLDDALEPRQASQGMVGQLAARRAAGVVLEMIREGKIAGRAVLIAGQPGTGKTAIAMGMAQALGPDTPFTAIAGSEIFSLEMSKTEALTQAFRRSIGVRIKEETEIIEGEVVEIQIDRPATGTGSKVGKLTLKTTEMETIYDLGTKMIESLTKDKVQAGDVITIDKATGKISKLGRSFTRARDYDAMGSQTKFVQCPDGELQKRKEVVHTVSLHEIDVINSRTQGFLALFSGDTGEIKSEVREQINAKVAEWREEGKAEIIPGVLFIDEVHMLDIESFSFLNRALESDMAPVLIMATNRGITRIRGTSYQSPHGIPIDLLDRLLIVSTTPYSEKDTKQILRIRCEEEDVEMSEDAYTVLTRIGLETSLRYAIQLITAASLVCRKRKGTEVQVDDIKRVYSLFLDESRSTQYMKEYQDAFLFNELKGETMDTS
uniprot
proteins
ec_number
3.6.4.12
uniprot
proteins
function
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). {ECO:0000269|PubMed:10428817, ECO:0000269|PubMed:10882073, ECO:0000269|PubMed:11713276, 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:25652260, ECO:0000269|PubMed:28561026, ECO:0000269|PubMed:33205750}.
uniprot
proteins
mass_dalton
51157
uniprot
proteins
mutagenesis
MUTAGEN 83; /note="K->M: No effect on interaction with NOPCHAP1."; /evidence="ECO:0000269|PubMed:33367824"; MUTAGEN 299; /note="D->N: Abolishes ATPase activity."; /evidence="ECO:0000269|PubMed:17157868"; MUTAGEN 300; /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
10810093
uniprot
proteins
pubmed
10882073
uniprot
proteins
pubmed
10966108
uniprot
proteins
pubmed
10998447
uniprot
proteins
pubmed
11080158
uniprot
proteins
pubmed
11230166
uniprot
proteins
pubmed
11713276
uniprot
proteins
pubmed
12665801
uniprot
proteins
pubmed
12963728
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14966270
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16014379
uniprot
proteins
pubmed
16230350
uniprot
proteins
pubmed
17157868
uniprot
proteins
pubmed
17967892
uniprot
proteins
pubmed
18026119
uniprot
proteins
pubmed
19299493
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19433865
uniprot
proteins
pubmed
20801936
uniprot
proteins
pubmed
20864032
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21303910
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24463511
uniprot
proteins
pubmed
25437307
uniprot
proteins
pubmed
25652260
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26812014
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28561026
uniprot
proteins
pubmed
29601588
uniprot
proteins
pubmed
30337683
uniprot
proteins
pubmed
31121004
uniprot
proteins
pubmed
31738558
uniprot
proteins
pubmed
33205750
uniprot
proteins
pubmed
33367824
uniprot
proteins
sequence_length
463
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm. Membrane. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE27}. 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.
uniprot
proteins