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UniProtKB - Q9Y230 (RUVB2_HUMAN)

Entry version 232 (29 Sep 2021)
Sequence version 3 (23 Jan 2007)
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Protein

RuvB-like 2

Gene

RUVBL2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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).

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).

11 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi77 – 84ATP8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, Chromatin regulator, Helicase, Hydrolase
Biological processDNA damage, DNA recombination, DNA repair, Growth regulation, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		Q9Y230

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-171319, Telomere Extension By Telomerase
R-HSA-3214847, HATs acetylate histones

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
RuvB-like 2 (EC:3.6.4.122 Publications)
Alternative name(s):
48 kDa TATA box-binding protein-interacting protein
Short name:
48 kDa TBP-interacting protein
51 kDa erythrocyte cytosolic protein
Short name:
ECP-51
INO80 complex subunit J
Repressing pontin 52
Short name:
Reptin 52
TIP49b
TIP60-associated protein 54-beta
Short name:
TAP54-beta
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RUVBL2
Synonyms:INO80J, TIP48, TIP49B
ORF Names:CGI-46
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 19

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:10475, RUVBL2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		604788, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_Q9Y230

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000183207

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi83K → M: No effect on interaction with NOPCHAP1. 1 Publication1
Mutagenesisi299D → N: Abolishes ATPase activity. 1 Publication1
Mutagenesisi300E → Q: Decreases interaction with NOPCHAP1. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		10856

Open Targets

More...OpenTargetsi		ENSG00000183207

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34888

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		Q9Y230, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2062349

Drug and drug target database

More...DrugBanki		DB04216, Quercetin

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RUVBL2

Domain mapping of disease mutations (DMDM)

More...DMDMi		28201890

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources2 Publications
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001656442 – 463RuvB-like 2Add BLAST462

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki9Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei437PhosphoserineCombined sources1
Cross-linki444Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki456Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

More...CPTACi		CPTAC-270
CPTAC-271

Encyclopedia of Proteome Dynamics

More...EPDi		Q9Y230

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		Q9Y230

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		Q9Y230

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		Q9Y230

PeptideAtlas

More...PeptideAtlasi		Q9Y230

PRoteomics IDEntifications database

More...PRIDEi		Q9Y230

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		3549
85619 [Q9Y230-1]

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00009104

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...GlyGeni		Q9Y230, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		Q9Y230

MetOSite database of methionine sulfoxide sites

More...MetOSitei		Q9Y230

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		Q9Y230

SwissPalm database of S-palmitoylation events

More...SwissPalmi		Q9Y230

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Ubiquitously expressed. Highly expressed in testis and thymus.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000183207, Expressed in testis and 238 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		Q9Y230, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		Q9Y230, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000183207, Tissue enhanced (testis)

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Forms homohexameric rings (Probable). Can form a dodecamer with RUVBL1 made of two stacked hexameric rings; however, even though RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric status of each hexamer is not known. Oligomerization may regulate binding to nucleic acids and conversely, binding to nucleic acids may affect the dodecameric assembly.

Interacts with the transcriptional activation domain of MYC.

Interacts With ATF2. Component of the RNA polymerase II holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A protein. RUVBL2 interacts with EP400.

Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.

Interacts with NPAT.

Component of the chromatin-remodeling INO80 complex; specifically part of a complex module associated with the helicase ATP-binding and the helicase C-terminal domain of INO80.

Component of some MLL1/MLL complex, at least composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10.

Interacts with IGHMBP2.

Interacts with TELO2.

Interacts with HINT1.

Component of a SWR1-like complex.

Component of the R2TP complex composed at least of RUVBL1, RUVBL2, RPAP3 and PIHD1 (PubMed:20864032).

Component of the PAQosome complex which is responsible for the biogenesis of several protein complexes and which consists of R2TP complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).

Interacts with ITFG1 (PubMed:25437307).

Interacts with ZMYND10 (PubMed:29601588).

Interacts with WAC; WAC positively regulates MTOR activity by promoting the assembly of the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of the mTORC1 complex and its subsequent activation (PubMed:26812014).

Forms a complex with APPL1 and APPL2 (PubMed:19433865).

Interacts with ZNHIT2 (via HIT-type zinc finger) in the presence of ATP or ADP; shows a stronger interaction in the presence of ADP (PubMed:28561026). The RUVBL1/RUVBL2 complex interacts with ZNHIT1 (via HIT-type zinc finger), ZNHIT3 (via HIT-type zinc finger), ZNHIT6 (via HIT-type zinc finger) and DDX59/ZNHIT5 (via HIT-type zinc finger) in the presence of ADP (PubMed:28561026).

Interacts with NOPCHAP1; the interaction is direct and disrupted upon ATP binding (PubMed:33367824).

Curated24 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		116067, 388 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-6143, R2TP core co-chaperone complex
CPX-6150, R2SP co-chaperone complex
CPX-6152, R2SD co-chaperone complex
CPX-6153, R2T co-chaperone complex
CPX-846, INO80 chromatin remodeling complex
CPX-974, SRCAP chromatin remodeling complex
CPX-978, NuA4 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		Q9Y230

Database of interacting proteins

More...DIPi		DIP-28153N

Protein interaction database and analysis system

More...IntActi		Q9Y230, 199 interactors

Molecular INTeraction database

More...MINTi		Q9Y230

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000473172

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		Q9Y230, protein

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1463
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		Q9Y230

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		Q9Y230

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal domain is required for association with ATF2.

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the RuvB family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG2680, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000153556

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_028311_4_0_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		Q9Y230

Identification of Orthologs from Complete Genome Data

More...OMAi		YDMGAKM

Database of Orthologous Groups

More...OrthoDBi		752343at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		Q9Y230

TreeFam database of animal gene trees

More...TreeFami		TF300469

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.50.360, 1 hit
3.40.50.300, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR003593, AAA+_ATPase
IPR027417, P-loop_NTPase
IPR027238, RuvB-like
IPR041048, RuvB-like_C
IPR042487, RuvBL1/2_DNA/RNA_bd_dom
IPR037942, RUVBL2
IPR010339, TIP49_P-loop

The PANTHER Classification System

More...PANTHERi		PTHR11093, PTHR11093, 1 hit
PTHR11093:SF2, PTHR11093:SF2, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF06068, TIP49, 1 hit
PF17856, TIP49_C, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF52540, SSF52540, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 8 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Y230-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL 
        60         70         80         90        100
AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF 
       110        120        130        140        150
TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP 
       160        170        180        190        200
ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG 
       210        220        230        240        250
KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH TVSLHEIDVI 
       260        270        280        290        300
NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 
       310        320        330        340        350
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL 
       360        370        380        390        400
LDRLLIVSTT PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR 
       410        420        430        440        450
YAIQLITAAS LVCRKRKGTE VQVDDIKRVY SLFLDESRST QYMKEYQDAF 
       460 
LFNELKGETM DTS
Length:463
Mass (Da):51,157
Last modified:January 23, 2007 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i54C78E9C587D975A
GO
Isoform 2 (identifier: Q9Y230-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-45: Missing.

Show »
Length:418
Mass (Da):46,306
Checksum:i64C304B804D86B2E
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 8 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
M0R0Y3M0R0Y3_HUMAN
RuvB-like helicase
RUVBL2
354Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
X6R2L4X6R2L4_HUMAN
RuvB-like helicase
RUVBL2
259Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QXI6M0QXI6_HUMAN
RuvB-like helicase
RUVBL2
109Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0R0Z0M0R0Z0_HUMAN
RuvB-like 2
RUVBL2
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QXZ7M0QXZ7_HUMAN
RuvB-like 2
RUVBL2 hCG_16214
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
M0QYD8M0QYD8_HUMAN
RuvB-like 2
RUVBL2 hCG_16214
44Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1W2PS48A0A1W2PS48_HUMAN
RuvB-like 2
RUVBL2
50Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A1W2PS22A0A1W2PS22_HUMAN
RuvB-like 2
RUVBL2
39Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAD34041 differs from that shown. Reason: Frameshift.Curated
The sequence AAH08355 differs from that shown. Reason: Frameshift.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti214D → N in AAD34041 (PubMed:10810093).Curated1
Sequence conflicti257 – 258FL → YV AA sequence (PubMed:10882073).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0565841 – 45Missing in isoform 2. 1 PublicationAdd BLAST45

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
Y18417 mRNA Translation: CAB46270.1
AB024301 mRNA Translation: BAA76708.1
AF155138 mRNA Translation: AAD38073.1
AF124607 mRNA Translation: AAF87087.1
AF151804 mRNA Translation: AAD34041.1 Frameshift.
AL136743 mRNA Translation: CAB66677.1
AK057498 mRNA Translation: BAG51921.1
AK074542 mRNA Translation: BAC11048.1
CR533507 mRNA Translation: CAG38538.1
AC008687 Genomic DNA No translation available.
CH471177 Genomic DNA Translation: EAW52426.1
CH471177 Genomic DNA Translation: EAW52430.1
BC000428 mRNA Translation: AAH00428.1
BC004531 mRNA Translation: AAH04531.1
BC008355 mRNA Translation: AAH08355.1 Frameshift.

The Consensus CDS (CCDS) project

More...CCDSi		CCDS42588.1 [Q9Y230-1]

Protein sequence database of the Protein Information Resource

More...PIRi		T46313

NCBI Reference Sequences

More...RefSeqi		NP_001308120.1, NM_001321191.1 [Q9Y230-2]
NP_006657.1, NM_006666.2 [Q9Y230-1]
XP_011524632.1, XM_011526330.1 [Q9Y230-2]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000595090; ENSP00000473172; ENSG00000183207 [Q9Y230-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		10856

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:10856

UCSC genome browser

More...UCSCi		uc002plr.2, human [Q9Y230-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Y18417 mRNA Translation: CAB46270.1
AB024301 mRNA Translation: BAA76708.1
AF155138 mRNA Translation: AAD38073.1
AF124607 mRNA Translation: AAF87087.1
AF151804 mRNA Translation: AAD34041.1 Frameshift.
AL136743 mRNA Translation: CAB66677.1
AK057498 mRNA Translation: BAG51921.1
AK074542 mRNA Translation: BAC11048.1
CR533507 mRNA Translation: CAG38538.1
AC008687 Genomic DNA No translation available.
CH471177 Genomic DNA Translation: EAW52426.1
CH471177 Genomic DNA Translation: EAW52430.1
BC000428 mRNA Translation: AAH00428.1
BC004531 mRNA Translation: AAH04531.1
BC008355 mRNA Translation: AAH08355.1 Frameshift.
CCDSiCCDS42588.1 [Q9Y230-1]
PIRiT46313
RefSeqiNP_001308120.1, NM_001321191.1 [Q9Y230-2]
NP_006657.1, NM_006666.2 [Q9Y230-1]
XP_011524632.1, XM_011526330.1 [Q9Y230-2]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2CQANMR-A132-213[»]
2XSZX-ray3.00D/E/F2-133[»]
D/E/F238-463[»]
3UK6X-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-132[»]
A/B/C/D/E/F/G/H/I/J/K/L239-463[»]
5OAFelectron microscopy4.06B/D/F1-463[»]
6FO1electron microscopy3.57D/E/F1-463[»]
6H7XX-ray2.89A1-463[»]
6HTSelectron microscopy4.80B/D/F1-463[»]
6IGMelectron microscopy4.00B/D/F1-463[»]
6K0RX-ray2.50D/E/F/J/K/L1-133[»]
D/E/F/J/K/L238-463[»]
6QI8electron microscopy3.75D/E/F1-463[»]
6QI9electron microscopy4.63D/E/F1-463[»]
7AHOelectron microscopy4.18D/E/F1-463[»]
SMRiQ9Y230
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi116067, 388 interactors
ComplexPortaliCPX-6143, R2TP core co-chaperone complex
CPX-6150, R2SP co-chaperone complex
CPX-6152, R2SD co-chaperone complex
CPX-6153, R2T co-chaperone complex
CPX-846, INO80 chromatin remodeling complex
CPX-974, SRCAP chromatin remodeling complex
CPX-978, NuA4 histone acetyltransferase complex
CORUMiQ9Y230
DIPiDIP-28153N
IntActiQ9Y230, 199 interactors
MINTiQ9Y230
STRINGi9606.ENSP00000473172

Chemistry databases

ChEMBLiCHEMBL2062349
DrugBankiDB04216, Quercetin

PTM databases

GlyGeniQ9Y230, 1 site, 1 O-linked glycan (1 site)
iPTMnetiQ9Y230
MetOSiteiQ9Y230
PhosphoSitePlusiQ9Y230
SwissPalmiQ9Y230

Genetic variation databases

BioMutaiRUVBL2
DMDMi28201890

2D gel databases

REPRODUCTION-2DPAGEiIPI00009104

Proteomic databases

CPTACiCPTAC-270
CPTAC-271
EPDiQ9Y230
jPOSTiQ9Y230
MassIVEiQ9Y230
PaxDbiQ9Y230
PeptideAtlasiQ9Y230
PRIDEiQ9Y230
ProteomicsDBi3549
85619 [Q9Y230-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		3244, 408 antibodies

The DNASU plasmid repository

More...DNASUi		10856

Genome annotation databases

EnsembliENST00000595090; ENSP00000473172; ENSG00000183207 [Q9Y230-1]
GeneIDi10856
KEGGihsa:10856
UCSCiuc002plr.2, human [Q9Y230-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		10856
DisGeNETi10856

GeneCards: human genes, protein and diseases

More...GeneCardsi		RUVBL2
HGNCiHGNC:10475, RUVBL2
HPAiENSG00000183207, Tissue enhanced (testis)
MIMi604788, gene
neXtProtiNX_Q9Y230
OpenTargetsiENSG00000183207
PharmGKBiPA34888
VEuPathDBiHostDB:ENSG00000183207

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG2680, Eukaryota
GeneTreeiENSGT00940000153556
HOGENOMiCLU_028311_4_0_1
InParanoidiQ9Y230
OMAiYDMGAKM
OrthoDBi752343at2759
PhylomeDBiQ9Y230
TreeFamiTF300469

Enzyme and pathway databases

PathwayCommonsiQ9Y230
ReactomeiR-HSA-171319, Telomere Extension By Telomerase
R-HSA-3214847, HATs acetylate histones

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		10856, 800 hits in 991 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		RUVBL2, human
EvolutionaryTraceiQ9Y230

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RUVBL2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		10856
PharosiQ9Y230, Tbio

Protein Ontology

More...PROi		PR:Q9Y230
RNActiQ9Y230, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000183207, Expressed in testis and 238 other tissues
ExpressionAtlasiQ9Y230, baseline and differential
GenevisibleiQ9Y230, HS

Family and domain databases

Gene3Di2.40.50.360, 1 hit
3.40.50.300, 1 hit
InterProiView protein in InterPro
IPR003593, AAA+_ATPase
IPR027417, P-loop_NTPase
IPR027238, RuvB-like
IPR041048, RuvB-like_C
IPR042487, RuvBL1/2_DNA/RNA_bd_dom
IPR037942, RUVBL2
IPR010339, TIP49_P-loop
PANTHERiPTHR11093, PTHR11093, 1 hit
PTHR11093:SF2, PTHR11093:SF2, 1 hit
PfamiView protein in Pfam
PF06068, TIP49, 1 hit
PF17856, TIP49_C, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRUVB2_HUMAN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y230
Secondary accession number(s): B3KQ59
, E7ETE5, Q6FIB9, Q6PK27, Q9Y361
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: January 23, 2007
Last modified: September 29, 2021
This is version 232 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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