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Q9Y265

- RUVB1_HUMAN

UniProt

Q9Y265 - RUVB1_HUMAN

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Protein
RuvB-like 1
Gene
RUVBL1, INO80H, NMP238, TIP49, TIP49A
Organism
Homo sapiens (Human)
Status
Reviewed - 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.7 Publications
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.7 Publications
Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair.7 Publications
Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation.7 Publications
May be able to bind plasminogen at cell surface and enhance plasminogen activation.7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi70 – 778ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA helicase activity Source: UniProtKB
  3. protein binding Source: UniProtKB

GO - Biological processi

  1. DNA duplex unwinding Source: GOC
  2. DNA recombination Source: UniProtKB-KW
  3. DNA repair Source: UniProtKB-KW
  4. centromere-specific nucleosome assembly Source: Reactome
  5. chromatin organization Source: Reactome
  6. histone H2A acetylation Source: UniProtKB
  7. histone H4 acetylation Source: UniProtKB
  8. mitotic nuclear division Source: UniProtKB-KW
  9. nucleosome assembly Source: Reactome
  10. regulation of growth Source: UniProtKB-KW
  11. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  12. spermatogenesis Source: ProtInc
  13. 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

ReactomeiREACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_7974. Telomere Extension By Telomerase.

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
ProteomesiUP000005640: 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.2 Publications

GO - Cellular componenti

  1. Golgi apparatus Source: HPA
  2. Ino80 complex Source: UniProtKB
  3. MLL1 complex Source: UniProtKB
  4. NuA4 histone acetyltransferase complex Source: UniProtKB
  5. Swr1 complex Source: UniProtKB
  6. cytoplasm Source: HPA
  7. extracellular vesicular exosome Source: UniProt
  8. intracellular membrane-bounded organelle Source: HPA
  9. membrane Source: UniProtKB-SubCell
  10. microtubule organizing center Source: UniProtKB-SubCell
  11. nuclear matrix Source: UniProtKB-SubCell
  12. nucleoplasm Source: Reactome
  13. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi302 – 3021D → N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation. 4 Publications

Organism-specific databases

PharmGKBiPA34887.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 456456RuvB-like 1
PRO_0000165639Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei453 – 4531N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9Y265.
PaxDbiQ9Y265.
PeptideAtlasiQ9Y265.
PRIDEiQ9Y265.

2D gel databases

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

PTM databases

PhosphoSiteiQ9Y265.

Expressioni

Tissue specificityi

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

Gene expression databases

ArrayExpressiQ9Y265.
BgeeiQ9Y265.
CleanExiHS_RUVBL1.
GenevestigatoriQ9Y265.

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.19 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
DKC1O608328EBI-353675,EBI-713091
RUVBL2Q9Y23021EBI-353675,EBI-352939
TERTO1474611EBI-353675,EBI-1772203
VPS72Q159066EBI-353675,EBI-399189
YY1P254904EBI-353675,EBI-765538

Protein-protein interaction databases

BioGridi114166. 158 interactions.
DIPiDIP-29937N.
IntActiQ9Y265. 71 interactions.
MINTiMINT-1138777.
STRINGi9606.ENSP00000318297.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 167
Turni17 – 204
Beta strandi28 – 303
Beta strandi34 – 363
Beta strandi39 – 413
Helixi43 – 5715
Beta strandi65 – 695
Beta strandi72 – 754
Helixi76 – 8712
Beta strandi93 – 975
Helixi98 – 1014
Beta strandi104 – 1063
Helixi108 – 11811
Beta strandi119 – 14022
Beta strandi157 – 1637
Beta strandi166 – 1727
Helixi174 – 1829
Beta strandi189 – 1946
Turni195 – 1973
Beta strandi200 – 2067
Beta strandi216 – 2216
Beta strandi228 – 23912
Helixi240 – 2456
Helixi278 – 28811
Beta strandi291 – 2966
Beta strandi298 – 3036
Helixi304 – 3063
Helixi309 – 31810
Beta strandi326 – 3316
Beta strandi334 – 3374
Beta strandi345 – 3473
Helixi352 – 3554
Beta strandi358 – 3625
Helixi368 – 38215
Helixi388 – 40013
Helixi403 – 4086
Helixi410 – 41910
Beta strandi423 – 4253
Helixi427 – 43610
Helixi440 – 4489

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9OX-ray2.20A/B/C1-456[»]
2XSZX-ray3.00A/B/C2-126[»]
A/B/C234-456[»]
ProteinModelPortaliQ9Y265.
SMRiQ9Y265. Positions 7-453.

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.

Phylogenomic databases

eggNOGiCOG1224.
HOVERGENiHBG054186.
InParanoidiQ9Y265.
KOiK04499.
OMAiNKVVSKY.
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. Align

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

MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG    50
VIVELIKSKK MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE 100
VYSTEIKKTE VLMENFRRAI GLRIKETKEV YEGEVTELTP CETENPMGGY 150
GKTISHVIIG LKTAKGTKQL KLDPSIFESL QKERVEAGDV IYIEANSGAV 200
KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL HDLDVANARP 250
QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF 300
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI 350
PLDLLDRVMI IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK 400
TTLRYSVQLL TPANLLAKIN GKDSIEKEHV EEISELFYDA KSSAKILADQ 450
QDKYMK 456
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei374 – 38613IIKIR…EGINI → VLSAAADPGQLAC in isoform 2.
VSP_021387Add
BLAST
Alternative sequencei387 – 45670Missing in isoform 2.
VSP_021388Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521I → T in BAD96283. 1 Publication
Sequence conflicti145 – 1451N → D in BAD96295. 1 Publication
Sequence conflicti285 – 2851K → R in ABF13334. 1 Publication
Sequence conflicti353 – 3531D → P in ABF13334. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_003698.1. NM_003707.2. [Q9Y265-1]
UniGeneiHs.272822.

Genome annotation databases

EnsembliENST00000322623; ENSP00000318297; ENSG00000175792. [Q9Y265-1]
ENST00000417360; ENSP00000393755; ENSG00000175792. [Q9Y265-2]
GeneIDi8607.
KEGGihsa:8607.
UCSCiuc003ekh.3. human. [Q9Y265-1]
uc010hss.3. human. [Q9Y265-2]

Polymorphism databases

DMDMi28201891.

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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS3047.1. [Q9Y265-1 ]
PIRi JE0334.
RefSeqi NP_003698.1. NM_003707.2. [Q9Y265-1 ]
UniGenei Hs.272822.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C9O X-ray 2.20 A/B/C 1-456 [» ]
2XSZ X-ray 3.00 A/B/C 2-126 [» ]
A/B/C 234-456 [» ]
ProteinModelPortali Q9Y265.
SMRi Q9Y265. Positions 7-453.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114166. 158 interactions.
DIPi DIP-29937N.
IntActi Q9Y265. 71 interactions.
MINTi MINT-1138777.
STRINGi 9606.ENSP00000318297.

PTM databases

PhosphoSitei Q9Y265.

Polymorphism databases

DMDMi 28201891.

2D gel databases

OGPi Q9Y265.
REPRODUCTION-2DPAGE Q9Y265.
SWISS-2DPAGE Q9Y265.

Proteomic databases

MaxQBi Q9Y265.
PaxDbi Q9Y265.
PeptideAtlasi Q9Y265.
PRIDEi Q9Y265.

Protocols and materials databases

DNASUi 8607.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000322623 ; ENSP00000318297 ; ENSG00000175792 . [Q9Y265-1 ]
ENST00000417360 ; ENSP00000393755 ; ENSG00000175792 . [Q9Y265-2 ]
GeneIDi 8607.
KEGGi hsa:8607.
UCSCi uc003ekh.3. human. [Q9Y265-1 ]
uc010hss.3. human. [Q9Y265-2 ]

Organism-specific databases

CTDi 8607.
GeneCardsi GC03M127783.
HGNCi HGNC:10474. RUVBL1.
HPAi HPA019947.
HPA019948.
MIMi 603449. gene.
neXtProti NX_Q9Y265.
PharmGKBi PA34887.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1224.
HOVERGENi HBG054186.
InParanoidi Q9Y265.
KOi K04499.
OMAi NKVVSKY.
PhylomeDBi Q9Y265.
TreeFami TF300457.

Enzyme and pathway databases

Reactomei REACT_172610. HATs acetylate histones.
REACT_197820. HATs acetylate histones.
REACT_200753. formation of the beta-catenin:TCF transactivating complex.
REACT_22186. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_7974. Telomere Extension By Telomerase.

Miscellaneous databases

ChiTaRSi RUVBL1. human.
EvolutionaryTracei Q9Y265.
GeneWikii RuvB-like_1.
GenomeRNAii 8607.
NextBioi 32249.
PROi Q9Y265.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9Y265.
Bgeei Q9Y265.
CleanExi HS_RUVBL1.
Genevestigatori Q9Y265.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view ]
PANTHERi PTHR11093. PTHR11093. 1 hit.
Pfami PF06068. TIP49. 1 hit.
[Graphical view ]
SMARTi SM00382. AAA. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "TIP49, homologous to the bacterial DNA helicase RuvB, acts as an autoantigen in human."
    Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S., Kishimoto T., Tamura T.-A.
    Biochem. Biophys. Res. Commun. 245:819-823(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Identification and characterization of the ubiquitously occurring nuclear matrix protein NMP 238."
    Holzmann K., Gerner C., Korosec T., Poeltl A., Grimm R., Sauermann G.
    Biochem. Biophys. Res. Commun. 252:39-45(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 1-7.
    Tissue: Pancreas.
  3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  4. "Pontin52, an interaction partner of beta-catenin, binds to the TATA box binding protein."
    Bauer A., Huber O., Kemler R.
    Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Colon adenocarcinoma.
  5. "Isolation, molecular characterization, and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic proteins."
    Salzer U., Kubicek M., Prohaska R.
    Biochim. Biophys. Acta 1446:365-370(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 34-46; 108-118; 169-177; 207-219 AND 446-456.
    Tissue: Bone marrow.
  6. "Purification, cloning, and characterization of a profibrinolytic plasminogen-binding protein, TIP49a."
    Hawley S.B., Tamura T.-A., Miles L.A.
    J. Biol. Chem. 276:179-186(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182 AND 184-201, FUNCTION.
  7. "The genomic structure of the human pontin 52 gene."
    Huber O., Orso S.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
  8. "RUVBL1-FK- splice variant."
    Koc F., Gartner W., Birkenkamp-Demtroeder K., Altenberger T., Daneva T., Wagner L.
    Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  9. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  10. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Cerebellum.
  11. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adipose tissue and Coronary artery.
  12. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  13. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  14. Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 23-33; 65-90; 153-162; 172-182; 318-333; 340-357; 363-372 AND 379-400, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  15. "An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc."
    Wood M.A., McMahon S.B., Cole M.D.
    Mol. Cell 5:321-330(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-33 AND 77-90, INTERACTION WITH MYC, MUTAGENESIS OF ASP-302.
  16. "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
    Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
    J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 23-33; 34-46; 77-90; 172-182; 185-201; 340-357 AND 405-418 (ISOFORM 1), IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
    Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
    Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-46 AND 108-117, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin during mitosis."
    Gartner W., Rossbacher J., Zierhut B., Daneva T., Base W., Weissel M., Waldhausl W., Pasternack M.S., Wagner L.
    Cell Motil. Cytoskeleton 56:79-93(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 34-46, FUNCTION, INTERACTION WITH TUBULIN, SUBCELLULAR LOCATION.
    Tissue: Monocyte.
  19. "TIP49b, a new RuvB-like DNA helicase, is included in a complex together with another RuvB-like DNA helicase, TIP49a."
    Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A., Okazaki K., Morishita T., Tamura T.-A.
    J. Biol. Chem. 274:22437-22444(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RUVBL2.
  20. "Pontin52 and reptin52 function as antagonistic regulators of beta-catenin signalling activity."
    Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U., Aragnol D., Kemler R., Pradel J.
    EMBO J. 19:6121-6130(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  21. "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."
    Park J., Wood M.A., Cole M.D.
    Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN BAF53 COMPLEX WITH ACTL6A; SMARCA2 AND TRRAP.
  22. "TIP49 regulates beta-catenin-mediated neoplastic transformation and T-cell factor target gene induction via effects on chromatin remodeling."
    Feng Y., Lee N., Fearon E.R.
    Cancer Res. 63:8726-8734(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-302.
  23. "Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
    Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
    Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
  24. "Physical association and coordinate function of the H3 K4 methyltransferase MLL1 and the H4 K16 acetyltransferase MOF."
    Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J., Allis C.D., Chait B.T., Hess J.L., Roeder R.G.
    Cell 121:873-885(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MLL1/MLL COMPLEX.
  25. Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  26. "The histidine triad protein Hint1 interacts with Pontin and Reptin and inhibits TCF-beta-catenin-mediated transcription."
    Weiske J., Huber O.
    J. Cell Sci. 118:3117-3129(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HINT1, FUNCTION, SUBCELLULAR LOCATION.
  27. "Dodecameric structure and ATPase activity of the human TIP48/TIP49 complex."
    Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.
    J. Mol. Biol. 366:179-192(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, MUTAGENESIS OF ASP-302, ELECTRON MICROSCOPY OF THE RUVBL1-RUVBL2 HETEROMER.
  28. "Functional characterization of the OFD1 protein reveals a nuclear localization and physical interaction with subunits of a chromatin remodeling complex."
    Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S., Franco B.
    Mol. Biol. Cell 18:4397-4404(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH OFD1.
  29. "A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
    Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
    Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX, PROTEIN INTERACTION.
  30. "Transcriptional activation of histone genes requires NPAT-dependent recruitment of TRRAP-Tip60 complex to histone promoters during the G1/S phase transition."
    DeRan M., Pulvino M., Greene E., Su C., Zhao J.
    Mol. Cell. Biol. 28:435-447(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NPAT.
  31. "Biochemical and genetic evidence for a role of IGHMBP2 in the translational machinery."
    de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A., Mourelatos Z.
    Hum. Mol. Genet. 18:2115-2126(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IGHMBP2.
  32. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. "Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
    Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
    J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
  35. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  36. "USP49 deubiquitinates histone H2B and regulates cotranscriptional pre-mRNA splicing."
    Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S., Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M., Giles K.E., Ma L., Wang H.
    Genes Dev. 27:1581-1595(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH USP49 AND PSMC5.
  37. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
  38. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-302.

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: September 3, 2014
This is version 153 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

External Data

Dasty 3

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