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Protein

RuvB-like 1

Gene

RUVBL1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

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

GO - Molecular functioni

  • ATPase activity Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent 5'-3' DNA helicase activity Source: InterPro
  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • DNA helicase activity Source: UniProtKB

GO - Biological processi

  • beta-catenin-TCF complex assembly Source: Reactome
  • box C/D snoRNP assembly Source: GO_Central
  • cell division Source: UniProtKB-KW
  • CENP-A containing nucleosome assembly Source: Reactome
  • chromatin remodeling Source: GO_Central
  • DNA recombination Source: UniProtKB-KW
  • DNA repair Source: GO_Central
  • histone H2A acetylation Source: UniProtKB
  • histone H4 acetylation Source: UniProtKB
  • mitotic nuclear division Source: UniProtKB-KW
  • positive regulation of protein targeting to mitochondrion Source: ParkinsonsUK-UCL
  • positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
  • regulation of growth Source: UniProtKB-KW
  • regulation of mitophagy Source: ParkinsonsUK-UCL
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • spermatogenesis Source: ProtInc
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, Cell division, DNA damage, DNA recombination, DNA repair, Growth regulation, Mitosis, Transcription, Transcription regulation

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175792-MONOMER.
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

HGNCiHGNC:10474. RUVBL1.

Subcellular locationi

  • Nucleus matrix
  • Nucleusnucleoplasm
  • Cytoplasm
  • Membrane
  • Cytoplasmcytoskeletonmicrotubule organizing centercentrosome

  • Note: Mainly localized in the nucleus, associated with nuclear matrix or in the nuclear cytosol, although it is also present in the cytoplasm and associated with the cell membranes. In prophase and prometaphase it is located at the centrosome and the branching microtubule spindles. After mitotic nuclear membrane disintigration it accumulates at the centrosome and sites of tubulin polymerization. As cells pass through metaphase and into telophase it is located close to the centrosome at the early phase of tubulin polymerization. In anaphase it accumulates at the zone of tubule interdigitation. In telophase it is found at polar tubule overlap, and it reappears at the site of chromosomal decondensation in the daughter cells.

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • Ino80 complex Source: UniProtKB
  • intracellular membrane-bounded organelle Source: HPA
  • membrane Source: UniProtKB-SubCell
  • microtubule organizing center Source: UniProtKB-SubCell
  • MLL1 complex Source: UniProtKB
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear matrix Source: UniProtKB-SubCell
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • R2TP complex Source: UniProtKB
  • Swr1 complex Source: UniProtKB
Complete GO annotation...

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)Combined sources
Modified residuei453N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9Y265.
PaxDbiQ9Y265.
PeptideAtlasiQ9Y265.
PRIDEiQ9Y265.

2D gel databases

OGPiQ9Y265.
REPRODUCTION-2DPAGEQ9Y265.
SWISS-2DPAGEQ9Y265.

PTM databases

iPTMnetiQ9Y265.
PhosphoSitePlusiQ9Y265.
SwissPalmiQ9Y265.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000175792.
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).22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DKC1O608328EBI-353675,EBI-713091
ECDO959057EBI-353675,EBI-2557598
I79_017133G3I1832EBI-353675,EBI-10890180From a different organism.
OFD1O756653EBI-353675,EBI-716327
RUVBL2Q9Y23026EBI-353675,EBI-352939
TERTO1474611EBI-353675,EBI-1772203
VPS72Q159066EBI-353675,EBI-399189
YY1P254905EBI-353675,EBI-765538

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi114166. 217 interactors.
DIPiDIP-29937N.
IntActiQ9Y265. 92 interactors.
MINTiMINT-1138777.
STRINGi9606.ENSP00000318297.

Chemistry databases

BindingDBiQ9Y265.

Structurei

Secondary structure

1456
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi10 – 16Combined sources7
Turni17 – 20Combined sources4
Beta strandi28 – 30Combined sources3
Beta strandi34 – 36Combined sources3
Beta strandi39 – 41Combined sources3
Helixi43 – 57Combined sources15
Beta strandi65 – 69Combined sources5
Beta strandi72 – 75Combined sources4
Helixi76 – 87Combined sources12
Beta strandi93 – 97Combined sources5
Helixi98 – 101Combined sources4
Beta strandi104 – 106Combined sources3
Helixi108 – 118Combined sources11
Beta strandi119 – 140Combined sources22
Beta strandi157 – 163Combined sources7
Beta strandi166 – 172Combined sources7
Helixi174 – 182Combined sources9
Beta strandi189 – 194Combined sources6
Turni195 – 197Combined sources3
Beta strandi200 – 206Combined sources7
Beta strandi216 – 221Combined sources6
Beta strandi228 – 239Combined sources12
Helixi240 – 245Combined sources6
Helixi278 – 288Combined sources11
Beta strandi291 – 296Combined sources6
Beta strandi298 – 303Combined sources6
Helixi304 – 306Combined sources3
Helixi309 – 318Combined sources10
Beta strandi326 – 331Combined sources6
Beta strandi334 – 337Combined sources4
Beta strandi345 – 347Combined sources3
Helixi352 – 355Combined sources4
Beta strandi358 – 362Combined sources5
Helixi368 – 382Combined sources15
Helixi388 – 400Combined sources13
Helixi403 – 408Combined sources6
Helixi410 – 419Combined sources10
Beta strandi423 – 425Combined sources3
Helixi427 – 436Combined sources10
Helixi440 – 448Combined sources9

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[»]
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.
GeneTreeiENSGT00550000075043.
HOVERGENiHBG054186.
InParanoidiQ9Y265.
KOiK04499.
OMAiYSTSDME.
OrthoDBiEOG091G07C9.
PhylomeDBiQ9Y265.
TreeFamiTF300457.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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

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.
Hs.710868.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

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.
Hs.710868.

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[»]
ProteinModelPortaliQ9Y265.
SMRiQ9Y265.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114166. 217 interactors.
DIPiDIP-29937N.
IntActiQ9Y265. 92 interactors.
MINTiMINT-1138777.
STRINGi9606.ENSP00000318297.

Chemistry databases

BindingDBiQ9Y265.
ChEMBLiCHEMBL3259467.

PTM databases

iPTMnetiQ9Y265.
PhosphoSitePlusiQ9Y265.
SwissPalmiQ9Y265.

Polymorphism and mutation databases

BioMutaiRUVBL1.
DMDMi28201891.

2D gel databases

OGPiQ9Y265.
REPRODUCTION-2DPAGEQ9Y265.
SWISS-2DPAGEQ9Y265.

Proteomic databases

EPDiQ9Y265.
PaxDbiQ9Y265.
PeptideAtlasiQ9Y265.
PRIDEiQ9Y265.

Protocols and materials databases

DNASUi8607.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

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

Phylogenomic databases

eggNOGiKOG1942. Eukaryota.
COG1224. LUCA.
GeneTreeiENSGT00550000075043.
HOVERGENiHBG054186.
InParanoidiQ9Y265.
KOiK04499.
OMAiYSTSDME.
OrthoDBiEOG091G07C9.
PhylomeDBiQ9Y265.
TreeFamiTF300457.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000175792-MONOMER.
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.
PROiQ9Y265.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000175792.
CleanExiHS_RUVBL1.
ExpressionAtlasiQ9Y265. baseline and differential.
GenevisibleiQ9Y265. HS.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERiPTHR11093. PTHR11093. 1 hit.
PfamiPF06068. TIP49. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
ProtoNetiSearch...

Entry informationi

Entry nameiRUVB1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y265
Secondary accession number(s): B2R5S0
, P82276, Q1KMR0, Q53HK5, Q53HL7, Q53Y27, Q9BSX9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: November 1, 1999
Last modified: November 30, 2016
This is version 179 of the entry and version 1 of the sequence. [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

Miscellaneous

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

Keywords - Technical termi

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

Documents

  1. Human chromosome 3
    Human chromosome 3: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.