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Reviewed, UniProtKB/Swiss-Prot Q9Y265 (RUVB1_HUMAN)

Last modified February 9, 2010. Version 104. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    RuvB-like 1
    EC=3.6.1.-
Alternative name(s):
    49 kDa TATA box-binding protein-interacting protein
      Short name=49 kDa TBP-interacting protein
    TIP49a
    Pontin 52
    Nuclear matrix protein 238
      Short name=NMP 238
    54 kDa erythrocyte cytosolic protein
      Short name=ECP-54
    TIP60-associated protein 54-alpha
      Short name=TAP54-alpha
    INO80 complex subunit H
Gene names
Name: RUVBL1
Synonyms: INO80H, NMP238, TIP49, TIP49A
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (3' to 5') 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. RUVBL1 plays an essential role in oncogenic transformation by MYC and also modulates transcriptional activation by the LEF1/TCF1-CTNNB1 complex. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23

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

Essential for cell proliferation. Ref.6 Ref.18 Ref.20 Ref.22 Ref.23

Subunit structure

Forms homotypic and heterotypic interactions. Forms a multimeric complex with RUVBL2. 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 MLL, ASH2L, HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components C17orf49, CHD8, E2F6, HSP70, IN80C, KIAA1267, 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, at least composed of ACTL6A, ACTR5, ACTR8, RVBL1, RVBL2, INO80, INO80B, INO80C, INO80D and INO80E. Interacts with IGHMBP2. Ref.18 Ref.15 Ref.19 Ref.26 Ref.28

Subcellular location

Nucleus matrix. Nucleus › nucleoplasm. Cytoplasm. Membrane. Cytoplasm › cytoskeleton › centrosome. 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

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.

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Ontologies

Keywords
   Biological processCell cycle
Cell division
DNA recombination
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
Gene Ontology (GO)
   Biological processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

cell division

Inferred from electronic annotation. Source: UniProtKB-KW

histone H2A acetylation Ref.23

Inferred from direct assay. Source: UniProtKB

histone H4 acetylation Ref.23

Inferred from direct assay. Source: UniProtKB

mitosis

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter Ref.2

Traceable author statement. Source: ProtInc

spermatogenesis Ref.1

Traceable author statement. Source: ProtInc

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentMLL1 complex Ref.24

Inferred from direct assay. Source: UniProtKB

NuA4 histone acetyltransferase complex Ref.17 Ref.23

Inferred from direct assay. Source: UniProtKB

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

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

DNA helicase activity Ref.4

Inferred from direct assay. Source: UniProtKB

protein binding Ref.17 Ref.28

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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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.

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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 residue21N6-acetyllysine Ref.29
Modified residue4531N6-acetyllysine Ref.29

Natural variations

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

Experimental info

Mutagenesis3021D → N: Inhibition of MYC- and CTNNB1-mediated transformation. Ref.22 Ref.15
Sequence conflict521I → T in BAD96283. Ref.11
Sequence conflict1451N → D in BAD96295. Ref.11
Sequence conflict2851K → R in ABF13334. Ref.8
Sequence conflict3531D → P in ABF13334. Ref.8

Secondary structure

1 .............................................................. 456
Helix Strand Turn

Details...

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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.

Checksum: 6F19852DA93A435A
Show »

FASTA38642,127

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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: 9588198] [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: 9813143] [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: 9774387] [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: 9843967] [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: 10524211] [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: 11027681] [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: 14702039] [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: 19054851] [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: 15489334] [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, 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: 10882073] [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: 12963728] [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, 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: 10966108] [Abstract]
Cited for: PROTEIN SEQUENCE OF 34-46 AND 108-117, IDENTIFICATION IN NUA4 COMPLEX, 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: 14506706] [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: 10428817] [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: 11080158] [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: 11839798] [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: 14695187] [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: 14966270] [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: 15960975] [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: 16230350] [Abstract]
Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[26]"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: 17967892] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH NPAT.
[27]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[28]"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: 19299493] [Abstract]
Cited for: INTERACTION WITH IGHMBP2.
[29]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-2 AND LYS-453, MASS SPECTROMETRY.
+Additional computationally mapped references.

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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.
IPIIPI00021187.
IPI00788942.
PIRJE0334.
RefSeqNP_003698.1.
UniGeneHs.272822

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9OX-ray2.20A/B/C1-456[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29937N.
IntActQ9Y265. 69 interactions.
STRINGQ9Y265.

PTM databases

PhosphoSiteQ9Y265.

2-D gel databases

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

Proteomic databases

PeptideAtlasQ9Y265.
PRIDEQ9Y265.

Genome annotation databases

EnsemblENST00000322623; ENSP00000318297; ENSG00000175792; Homo sapiens. [Genome view]
GeneID8607.
KEGGhsa:8607.
UCSCuc003ekf.1. human.
uc003ekh.1. human.

Organism-specific databases

CTD8607.
GeneCardsGC03M129282.
H-InvDBHIX0021235.
HGNCHGNC:10474. RUVBL1.
HPAHPA019947.
HPA019948.
MIM603449. gene.
PharmGKBPA34887.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG09539.
HOVERGENQ9Y265.
InParanoidQ9Y265.
OMAKRVGRSD.
OrthoDBEOG9F4VW7.
PhylomeDBQ9Y265.

Gene expression databases

ArrayExpressQ9Y265.
BgeeQ9Y265.
CleanExHS_RUVBL1.
GenevestigatorQ9Y265.
GermOnlineENSG00000175792. Homo sapiens.

Family and domain databases

InterProIPR003593. ATPase_AAA+_core.
IPR010339. TIP49_C.
[Graphical view]
PfamPF06068. TIP49. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio32249.
SOURCESearch...

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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: February 9, 2010
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 3

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents