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Entry version 206 (18 Sep 2019)
Sequence version 1 (01 Nov 1999)
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Protein

RuvB-like 1

Gene

RUVBL1

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 (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.
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. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. 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. 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. Component of a SWR1-like complex that specifically mediates the removal of histone H2A.Z/H2AFZ from the nucleosome.
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.
Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation.
May be able to bind plasminogen at cell surface and enhance plasminogen activation.

Miscellaneous

High level of autoantibodies against RUVBL1 are detected in sera of patients with autoimmune diseases such as polymyositis/dermatomyosistis and autoimmune hepatitis.

<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 bindingi70 – 77ATPBy similarity8

<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

GO - Biological processi

<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 processCell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Growth regulation, Mitosis, Transcription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-171319 Telomere Extension By Telomerase
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-3214847 HATs acetylate histones
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere

<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 1 (EC:3.6.4.12)
Alternative name(s):
49 kDa TATA box-binding protein-interacting protein
Short name:
49 kDa TBP-interacting protein
54 kDa erythrocyte cytosolic protein
Short name:
ECP-54
INO80 complex subunit H
Nuclear matrix protein 238
Short name:
NMP 238
Pontin 52
TIP49a
TIP60-associated protein 54-alpha
Short name:
TAP54-alpha
<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:RUVBL1
Synonyms:INO80H, NMP238, TIP49, TIP49A
<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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<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 3

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:10474 RUVBL1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
603449 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q9Y265

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, 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>Mutagenesisi302D → N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation. 4 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
8607

Open Targets

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OpenTargetsi
ENSG00000175792

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA34887

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3259467

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
RUVBL1

Domain mapping of disease mutations (DMDM)

More...
DMDMi
28201891

<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 ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001656391 – 456RuvB-like 1Add BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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-linki2Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki225Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki445Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
<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 residuei453N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

The CPTAC Assay portal

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CPTACi
CPTAC-268
CPTAC-269

Encyclopedia of Proteome Dynamics

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EPDi
Q9Y265

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q9Y265

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9Y265

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

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PaxDbi
Q9Y265

PeptideAtlas

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PeptideAtlasi
Q9Y265

PRoteomics IDEntifications database

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PRIDEi
Q9Y265

ProteomicsDB human proteome resource

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ProteomicsDBi
85669 [Q9Y265-1]
85670 [Q9Y265-2]

2D gel databases

USC-OGP 2-DE database

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OGPi
Q9Y265

REPRODUCTION-2DPAGE

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REPRODUCTION-2DPAGEi
Q9Y265

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

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SWISS-2DPAGEi
Q9Y265

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9Y265

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

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PhosphoSitePlusi
Q9Y265

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9Y265

<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 with high expression in heart, skeletal muscle and testis.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000175792 Expressed in 206 organ(s), highest expression level in bronchial epithelial cell

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9Y265 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9Y265 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA019947
HPA019948

<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. Can form a dodecamer with RUVBL2 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.

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. RUVBL1 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.

Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and TRRAP/PAF400.

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. Associates with alpha and gamma tubulins, particularly during metaphase and early anaphase.

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.

Interacts with IGHMBP2.

Interacts with OFD1.

Interacts with HINT1.

Component of a complex with USP49 and PSMC5.

Component of a SWR1-like complex.

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

Interacts with PIH1D1 (PubMed:17636026).

Interacts with ITFG1 (PubMed:25437307).

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).

23 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
114166, 295 interactors

ComplexPortal: manually curated resource of macromolecular complexes

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ComplexPortali
CPX-846 INO80 chromatin remodeling complex
CPX-974 SRCAP histone exchanging complex
CPX-978 NuA4 histone acetyltransferase complex

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9Y265

Database of interacting proteins

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DIPi
DIP-29937N

Protein interaction database and analysis system

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IntActi
Q9Y265, 146 interactors

Molecular INTeraction database

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MINTi
Q9Y265

STRING: functional protein association networks

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STRINGi
9606.ENSP00000318297

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q9Y265

<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

1456
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

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SMRi
Q9Y265

Database of comparative protein structure models

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ModBasei
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q9Y265

<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

Binding to MYC is dependent on a Myc domain essential for oncogenic activity.

<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

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eggNOGi
KOG1942 Eukaryota
COG1224 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000153556

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9Y265

KEGG Orthology (KO)

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KOi
K04499

Identification of Orthologs from Complete Genome Data

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OMAi
LECFTYL

Database of Orthologous Groups

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OrthoDBi
752343at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9Y265

TreeFam database of animal gene trees

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TreeFami
TF300457

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR027238 RuvB-like
IPR041048 RuvB-like_C
IPR037938 RUVBL1
IPR010339 TIP49_P-loop

The PANTHER Classification System

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PANTHERi
PTHR11093 PTHR11093, 1 hit
PTHR11093:SF6 PTHR11093:SF6, 1 hit

Pfam protein domain database

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

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00382 AAA, 1 hit

Superfamily database of structural and functional annotation

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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.

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 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q9Y265-1) [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
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG
60 70 80 90 100
VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE
110 120 130 140 150
VYSTEIKKTE VLMENFRRAI GLRIKETKEV YEGEVTELTP CETENPMGGY
160 170 180 190 200
GKTISHVIIG LKTAKGTKQL KLDPSIFESL QKERVEAGDV IYIEANSGAV
210 220 230 240 250
KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL HDLDVANARP
260 270 280 290 300
QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF
310 320 330 340 350
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI
360 370 380 390 400
PLDLLDRVMI IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK
410 420 430 440 450
TTLRYSVQLL TPANLLAKIN GKDSIEKEHV EEISELFYDA KSSAKILADQ

QDKYMK
Length:456
Mass (Da):50,228
Last modified:November 1, 1999 - v1
<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:i6095ADE692B1482B
GO
Isoform 2 (identifier: Q9Y265-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     374-386: IIKIRAQTEGINI → VLSAAADPGQLAC
     387-456: Missing.

Show »
Length:386
Mass (Da):42,127
Checksum:i6F19852DA93A435A
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E7ETR0E7ETR0_HUMAN
RuvB-like helicase
RUVBL1
315Annotation 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>
H7C4I3H7C4I3_HUMAN
RuvB-like helicase
RUVBL1
222Annotation 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>
H7C4G5H7C4G5_HUMAN
RuvB-like helicase
RUVBL1
267Annotation 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>
J3QLR1J3QLR1_HUMAN
RuvB-like helicase
RUVBL1
131Annotation 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>

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 conflicti52I → T in BAD96283 (PubMed:19054851).Curated1
Sequence conflicti145N → D in BAD96295 (PubMed:19054851).Curated1
Sequence conflicti285K → R in ABF13334 (Ref. 8) Curated1
Sequence conflicti353D → P in ABF13334 (Ref. 8) Curated1

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_021387374 – 386IIKIR…EGINI → VLSAAADPGQLAC in isoform 2. 1 PublicationAdd BLAST13
Alternative sequenceiVSP_021388387 – 456Missing in isoform 2. 1 PublicationAdd BLAST70

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AB012122 mRNA Translation: BAA28169.1
AJ010058 mRNA Translation: CAA08986.1
AF070735 mRNA Translation: AAC77819.1
AF099084 mRNA Translation: AAD04427.1
Y18418 mRNA Translation: CAB46271.1
AF380344, AF380343 Genomic DNA Translation: AAM45570.1
DQ469310 mRNA Translation: ABF13334.1
BT007057 mRNA Translation: AAP35706.1
AK222563 mRNA Translation: BAD96283.1
AK222575 mRNA Translation: BAD96295.1
AK312290 mRNA Translation: BAG35217.1
AB451224 mRNA Translation: BAG70038.1
BC002993 mRNA Translation: AAH02993.1
BC012886 mRNA Translation: AAH12886.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS3047.1 [Q9Y265-1]

Protein sequence database of the Protein Information Resource

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PIRi
JE0334

NCBI Reference Sequences

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RefSeqi
NP_001306013.1, NM_001319084.1 [Q9Y265-2]
NP_003698.1, NM_003707.2 [Q9Y265-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000322623; ENSP00000318297; ENSG00000175792 [Q9Y265-1]
ENST00000643444; ENSP00000494621; ENSG00000284901 [Q9Y265-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
8607

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:8607

UCSC genome browser

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UCSCi
uc003ekh.4 human [Q9Y265-1]

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
AB012122 mRNA Translation: BAA28169.1
AJ010058 mRNA Translation: CAA08986.1
AF070735 mRNA Translation: AAC77819.1
AF099084 mRNA Translation: AAD04427.1
Y18418 mRNA Translation: CAB46271.1
AF380344, AF380343 Genomic DNA Translation: AAM45570.1
DQ469310 mRNA Translation: ABF13334.1
BT007057 mRNA Translation: AAP35706.1
AK222563 mRNA Translation: BAD96283.1
AK222575 mRNA Translation: BAD96295.1
AK312290 mRNA Translation: BAG35217.1
AB451224 mRNA Translation: BAG70038.1
BC002993 mRNA Translation: AAH02993.1
BC012886 mRNA Translation: AAH12886.1
CCDSiCCDS3047.1 [Q9Y265-1]
PIRiJE0334
RefSeqiNP_001306013.1, NM_001319084.1 [Q9Y265-2]
NP_003698.1, NM_003707.2 [Q9Y265-1]

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2C9OX-ray2.20A/B/C1-456[»]
2XSZX-ray3.00A/B/C2-126[»]
A/B/C234-456[»]
5OAFelectron microscopy4.06A/C/E1-456[»]
6FO1electron microscopy3.57A/B/C1-456[»]
6HTSelectron microscopy4.80A/C/E1-456[»]
6QI8electron microscopy3.75A/B/C1-456[»]
6QI9electron microscopy4.63A/B/C1-456[»]
SMRiQ9Y265
ModBaseiSearch...

Protein-protein interaction databases

BioGridi114166, 295 interactors
ComplexPortaliCPX-846 INO80 chromatin remodeling complex
CPX-974 SRCAP histone exchanging complex
CPX-978 NuA4 histone acetyltransferase complex
CORUMiQ9Y265
DIPiDIP-29937N
IntActiQ9Y265, 146 interactors
MINTiQ9Y265
STRINGi9606.ENSP00000318297

Chemistry databases

BindingDBiQ9Y265
ChEMBLiCHEMBL3259467

PTM databases

iPTMnetiQ9Y265
PhosphoSitePlusiQ9Y265
SwissPalmiQ9Y265

Polymorphism and mutation databases

BioMutaiRUVBL1
DMDMi28201891

2D gel databases

OGPiQ9Y265
REPRODUCTION-2DPAGEiQ9Y265
SWISS-2DPAGEiQ9Y265

Proteomic databases

CPTACiCPTAC-268
CPTAC-269
EPDiQ9Y265
jPOSTiQ9Y265
MassIVEiQ9Y265
PaxDbiQ9Y265
PeptideAtlasiQ9Y265
PRIDEiQ9Y265
ProteomicsDBi85669 [Q9Y265-1]
85670 [Q9Y265-2]

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
8607
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000322623; ENSP00000318297; ENSG00000175792 [Q9Y265-1]
ENST00000643444; ENSP00000494621; ENSG00000284901 [Q9Y265-1]
GeneIDi8607
KEGGihsa:8607
UCSCiuc003ekh.4 human [Q9Y265-1]

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
8607
DisGeNETi8607

GeneCards: human genes, protein and diseases

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GeneCardsi
RUVBL1
HGNCiHGNC:10474 RUVBL1
HPAiHPA019947
HPA019948
MIMi603449 gene
neXtProtiNX_Q9Y265
OpenTargetsiENSG00000175792
PharmGKBiPA34887

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1942 Eukaryota
COG1224 LUCA
GeneTreeiENSGT00940000153556
InParanoidiQ9Y265
KOiK04499
OMAiLECFTYL
OrthoDBi752343at2759
PhylomeDBiQ9Y265
TreeFamiTF300457

Enzyme and pathway databases

ReactomeiR-HSA-171319 Telomere Extension By Telomerase
R-HSA-201722 Formation of the beta-catenin:TCF transactivating complex
R-HSA-3214847 HATs acetylate histones
R-HSA-5689603 UCH proteinases
R-HSA-5689880 Ub-specific processing proteases
R-HSA-5696394 DNA Damage Recognition in GG-NER
R-HSA-606279 Deposition of new CENPA-containing nucleosomes at the centromere

Miscellaneous databases

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

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ChiTaRSi
RUVBL1 human
EvolutionaryTraceiQ9Y265

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
RuvB-like_1

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

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GenomeRNAii
8607

Pharos

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Pharosi
Q9Y265

Protein Ontology

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PROi
PR:Q9Y265

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000175792 Expressed in 206 organ(s), highest expression level in bronchial epithelial cell
ExpressionAtlasiQ9Y265 baseline and differential
GenevisibleiQ9Y265 HS

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR027238 RuvB-like
IPR041048 RuvB-like_C
IPR037938 RUVBL1
IPR010339 TIP49_P-loop
PANTHERiPTHR11093 PTHR11093, 1 hit
PTHR11093:SF6 PTHR11093:SF6, 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

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiRUVB1_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: Q9Y265
Secondary accession number(s): B2R5S0
, P82276, Q1KMR0, Q53HK5, Q53HL7, Q53Y27, Q9BSX9
<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: November 1, 1999
Last modified: September 18, 2019
This is version 206 of the entry and version 1 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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