UniProt ID: P83571 |
FUNCTION: Has double-stranded DNA-stimulated ATPase activity (PubMed:12464178). Has ATP-dependent DNA helicase (5' to 3') activity suggesting a role in nuclear processes such as recombination and transcription (By similarity). Represses gene activation mediated by beta-catenin (PubMed:12464178). Proposed core component of the chromatin remodeling Ino80 complex which exhibits DNA- and nucleosome- activated ATPase activity and catalyzes ATP-dependent nucleosome sliding (By similarity). Involved in the endoplasmic reticulum (ER)- associated degradation (ERAD) pathway where it negatively regulates expression of ER stress response genes (By similarity). May act as a regulator of embryonic heart growth (PubMed:12464178). {ECO:0000250|UniProtKB:Q9Y230, ECO:0000269|PubMed:12464178}. CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; Evidence={ECO:0000269|PubMed:12464178}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; Evidence={ECO:0000305|PubMed:12464178}; SUBUNIT: Forms homohexameric rings (Probable). Can form a dodecamer with ruvbl1 made of two stacked hexameric rings (By similarity). Component of the chromatin-remodeling Ino80 complex (By similarity). Component of some MLL1/MLL complex (By similarity). {ECO:0000250|UniProtKB:Q9Y230, ECO:0000305}. SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE27}. DEVELOPMENTAL STAGE: Widely expressed in the embryo. After 60 hours post-fertilization there is increased expression in heart, liver, branchial arches, exocrine pancreas and intestine. {ECO:0000269|PubMed:12464178}. DISRUPTION PHENOTYPE: Fishes display embryonic cardiac hyperplasia with increased cell number and size by 72 hours post-fertilization. Gut and gut-derived organs are incapable of growth and differentiation after this time. The mutation enhances ATPase activity, rendering it DNA- independent and causes aggregation of the protein into large complexes. {ECO:0000269|PubMed:12464178}. SIMILARITY: Belongs to the RuvB family. {ECO:0000250|UniProtKB:Q9Y230}. |
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