Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

RuvB-like 1

Gene

RUVBL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi70 – 77ATPBy similarity8

GO - Molecular functioni

GO - Biological processi

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

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

Names & Taxonomyi

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
Gene namesi
Name:RUVBL1
Synonyms:INO80H, NMP238, TIP49, TIP49A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000175792.11
HGNCiHGNC:10474 RUVBL1
MIMi603449 gene
neXtProtiNX_Q9Y265

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; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi302D → N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation. 4 Publications1

Organism-specific databases

DisGeNETi8607
OpenTargetsiENSG00000175792
PharmGKBiPA34887

Chemistry databases

ChEMBLiCHEMBL3259467

Polymorphism and mutation databases

BioMutaiRUVBL1
DMDMi28201891

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001656391 – 456RuvB-like 1Add BLAST456

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Modified residuei453N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9Y265
PaxDbiQ9Y265
PeptideAtlasiQ9Y265
PRIDEiQ9Y265
ProteomicsDBi85669
85670 [Q9Y265-2]

2D gel databases

OGPiQ9Y265
REPRODUCTION-2DPAGEiQ9Y265
SWISS-2DPAGEiQ9Y265

PTM databases

iPTMnetiQ9Y265
PhosphoSitePlusiQ9Y265
SwissPalmiQ9Y265

Expressioni

Tissue specificityi

Ubiquitously expressed with high expression in heart, skeletal muscle and testis.

Gene expression databases

BgeeiENSG00000175792 Expressed in 206 organ(s), highest expression level in bronchial epithelial cell
CleanExiHS_RUVBL1
ExpressionAtlasiQ9Y265 baseline and differential
GenevisibleiQ9Y265 HS

Organism-specific databases

HPAiHPA019947
HPA019948

Interactioni

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

Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

BioGridi114166, 248 interactors
ComplexPortaliCPX-846 INO80 chromatin remodeling complex
CPX-974 SRCAP histone exchanging complex
CPX-978 NuA4 histone acetyltransferase complex
CORUMiQ9Y265
DIPiDIP-29937N
IntActiQ9Y265, 111 interactors
MINTiQ9Y265
STRINGi9606.ENSP00000318297

Chemistry databases

BindingDBiQ9Y265

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

ProteinModelPortaliQ9Y265
SMRiQ9Y265
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y265

Family & Domainsi

Domaini

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

Sequence similaritiesi

Belongs to the RuvB family.Curated

Phylogenomic databases

eggNOGiKOG1942 Eukaryota
COG1224 LUCA
GeneTreeiENSGT00890000139499
HOVERGENiHBG054186
InParanoidiQ9Y265
KOiK04499
OMAiDVHKRKE
OrthoDBiEOG091G07C9
PhylomeDBiQ9Y265
TreeFamiTF300457

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR027238 RuvB-like
IPR037938 RUVBL1
IPR010339 TIP49_C
PANTHERiPTHR11093 PTHR11093, 1 hit
PTHR11093:SF6 PTHR11093:SF6, 1 hit
PfamiView protein in Pfam
PF06068 TIP49, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 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 'canonical' 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
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

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:
H7C4I3H7C4I3_HUMAN
RuvB-like helicase
RUVBL1
222Annotation score:
H7C4G5H7C4G5_HUMAN
RuvB-like helicase
RUVBL1
267Annotation score:
J3QLR1J3QLR1_HUMAN
RuvB-like helicase
RUVBL1
131Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
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:
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]
UniGeneiHs.272822

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

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]
UniGeneiHs.272822

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
6ETXelectron microscopy4.80A/C/E1-456[»]
6FO1electron microscopy3.57A/B/C1-456[»]
ProteinModelPortaliQ9Y265
SMRiQ9Y265
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114166, 248 interactors
ComplexPortaliCPX-846 INO80 chromatin remodeling complex
CPX-974 SRCAP histone exchanging complex
CPX-978 NuA4 histone acetyltransferase complex
CORUMiQ9Y265
DIPiDIP-29937N
IntActiQ9Y265, 111 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

EPDiQ9Y265
PaxDbiQ9Y265
PeptideAtlasiQ9Y265
PRIDEiQ9Y265
ProteomicsDBi85669
85670 [Q9Y265-2]

Protocols and materials databases

DNASUi8607
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

CTDi8607
DisGeNETi8607
EuPathDBiHostDB:ENSG00000175792.11
GeneCardsiRUVBL1
HGNCiHGNC:10474 RUVBL1
HPAiHPA019947
HPA019948
MIMi603449 gene
neXtProtiNX_Q9Y265
OpenTargetsiENSG00000175792
PharmGKBiPA34887
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1942 Eukaryota
COG1224 LUCA
GeneTreeiENSGT00890000139499
HOVERGENiHBG054186
InParanoidiQ9Y265
KOiK04499
OMAiDVHKRKE
OrthoDBiEOG091G07C9
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

ChiTaRSiRUVBL1 human
EvolutionaryTraceiQ9Y265
GeneWikiiRuvB-like_1
GenomeRNAii8607
PROiPR:Q9Y265
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175792 Expressed in 206 organ(s), highest expression level in bronchial epithelial cell
CleanExiHS_RUVBL1
ExpressionAtlasiQ9Y265 baseline and differential
GenevisibleiQ9Y265 HS

Family and domain databases

InterProiView protein in InterPro
IPR003593 AAA+_ATPase
IPR027417 P-loop_NTPase
IPR027238 RuvB-like
IPR037938 RUVBL1
IPR010339 TIP49_C
PANTHERiPTHR11093 PTHR11093, 1 hit
PTHR11093:SF6 PTHR11093:SF6, 1 hit
PfamiView protein in Pfam
PF06068 TIP49, 1 hit
SMARTiView protein in SMART
SM00382 AAA, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiRUVB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y265
Secondary accession number(s): B2R5S0
, P82276, Q1KMR0, Q53HK5, Q53HL7, Q53Y27, Q9BSX9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: November 1, 1999
Last modified: November 7, 2018
This is version 198 of the entry and version 1 of the sequence. See complete history.
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again