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Q9Y265 (RUVB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RUVBL1
Synonyms:INO80H, NMP238, TIP49, TIP49A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length456 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Ref.37

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. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Ref.37

Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Ref.37

Plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Essential for cell proliferation. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Ref.37

May be able to bind plasminogen at cell surface and enhance plasminogen activation. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23 Ref.26 Ref.37

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.34 Ref.36 Ref.37 Ref.38

Subcellular location

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. Ref.18 Ref.26

Tissue specificity

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

Domain

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

Miscellaneous

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

Sequence similarities

Belongs to the RuvB family.

Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA damage
DNA recombination
DNA repair
Growth regulation
Mitosis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Cytoskeleton
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
   LigandATP-binding
Nucleotide-binding
   Molecular functionActivator
Chromatin regulator
Helicase
Hydrolase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processCENP-A containing nucleosome assembly at centromere

Traceable author statement. Source: Reactome

DNA duplex unwinding

Inferred from direct assay Ref.4. Source: GOC

DNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.23. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.23. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

nucleosome assembly

Traceable author statement. Source: Reactome

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Traceable author statement Ref.2. Source: ProtInc

spermatogenesis

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Ino80 complex

Inferred from direct assay Ref.29Ref.34. Source: UniProtKB

MLL1 complex

Inferred from direct assay Ref.24. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from direct assay Ref.17Ref.23. Source: UniProtKB

Swr1 complex

Inferred from direct assay Ref.37. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule organizing center

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.29Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y265-1)

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.
Isoform 2 (identifier: Q9Y265-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 456456RuvB-like 1
PRO_0000165639

Regions

Nucleotide binding70 – 778ATP By similarity

Amino acid modifications

Modified residue4531N6-acetyllysine Ref.32

Natural variations

Alternative sequence374 – 38613IIKIR…EGINI → VLSAAADPGQLAC in isoform 2.
VSP_021387
Alternative sequence387 – 45670Missing in isoform 2.
VSP_021388

Experimental info

Mutagenesis3021D → N: Abolishes ATPase activity; inhibition of MYC- and CTNNB1-mediated transformation. Ref.15 Ref.22 Ref.27 Ref.38
Sequence conflict521I → T in BAD96283. Ref.12
Sequence conflict1451N → D in BAD96295. Ref.12
Sequence conflict2851K → R in ABF13334. Ref.8
Sequence conflict3531D → P in ABF13334. Ref.8

Secondary structure

.......................................................................... 456
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 6095ADE692B1482B

FASTA45650,228
        10         20         30         40         50         60 
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK 

        70         80         90        100        110        120 
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI 

       130        140        150        160        170        180 
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL 

       190        200        210        220        230        240 
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL 

       250        260        270        280        290        300 
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF 

       310        320        330        340        350        360 
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI 

       370        380        390        400        410        420 
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN 

       430        440        450 
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK 

« Hide

Isoform 2 [UniParc].

Checksum: 6F19852DA93A435A
Show »

FASTA38642,127

References

« Hide 'large scale' references
[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]"An eukaryotic RuvB-like protein (RUVBL1) essential for growth."
Qiu X.-B., Lin Y.-L., Thome K.C., Pian P., Schlegel B.P., Weremowicz S., Parvin J.D., Dutta A.
J. Biol. Chem. 273:27786-27793(1998) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex."
Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K., Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P., Conaway R.C., Conaway J.W.
J. Biol. Chem. 280:41207-41212(2005) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
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]"ANP32E is a histone chaperone that removes H2A.Z from chromatin."
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C., Hamiche A.
Nature 505:648-653(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
[38]"Crystal structure of the human AAA+ protein RuvBL1."
Matias P.M., Gorynia S., Donner P., Carrondo M.A.
J. Biol. Chem. 281:38918-38929(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-302.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJE0334.
RefSeqNP_003698.1. NM_003707.2.
UniGeneHs.272822.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9OX-ray2.20A/B/C1-456[»]
2XSZX-ray3.00A/B/C2-456[»]
ProteinModelPortalQ9Y265.
SMRQ9Y265. Positions 7-453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114166. 168 interactions.
DIPDIP-29937N.
IntActQ9Y265. 71 interactions.
MINTMINT-1138777.
STRING9606.ENSP00000318297.

PTM databases

PhosphoSiteQ9Y265.

Polymorphism databases

DMDM28201891.

2D gel databases

OGPQ9Y265.
REPRODUCTION-2DPAGEQ9Y265.
SWISS-2DPAGEQ9Y265.

Proteomic databases

PaxDbQ9Y265.
PeptideAtlasQ9Y265.
PRIDEQ9Y265.

Protocols and materials databases

DNASU8607.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000322623; ENSP00000318297; ENSG00000175792. [Q9Y265-1]
ENST00000417360; ENSP00000393755; ENSG00000175792. [Q9Y265-2]
GeneID8607.
KEGGhsa:8607.
UCSCuc003ekh.3. human. [Q9Y265-1]
uc010hss.3. human. [Q9Y265-2]

Organism-specific databases

CTD8607.
GeneCardsGC03M127783.
HGNCHGNC:10474. RUVBL1.
HPAHPA019947.
HPA019948.
MIM603449. gene.
neXtProtNX_Q9Y265.
PharmGKBPA34887.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1224.
HOVERGENHBG054186.
InParanoidQ9Y265.
KOK04499.
OMANKVVSKY.
PhylomeDBQ9Y265.
TreeFamTF300457.

Enzyme and pathway databases

ReactomeREACT_115566. Cell Cycle.
REACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9Y265.
BgeeQ9Y265.
CleanExHS_RUVBL1.
GenevestigatorQ9Y265.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR003593. AAA+_ATPase.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERPTHR11093. PTHR11093. 1 hit.
PfamPF06068. TIP49. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
ProtoNetSearch...

Other

ChiTaRSRUVBL1. human.
EvolutionaryTraceQ9Y265.
GeneWikiRuvB-like_1.
GenomeRNAi8607.
NextBio32249.
PROQ9Y265.
SOURCESearch...

Entry information

Entry nameRUVB1_HUMAN
AccessionPrimary (citable) accession number: Q9Y265
Secondary accession number(s): B2R5S0 expand/collapse secondary AC list , P82276, Q1KMR0, Q53HK5, Q53HL7, Q53Y27, Q9BSX9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM