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Q9Y230

- RUVB2_HUMAN

UniProt

Q9Y230 - RUVB2_HUMAN

Protein

RuvB-like 2

Gene

RUVBL2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Possesses single-stranded DNA-stimulated ATPase and ATP-dependent DNA helicase (5' to 3') 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. May also inhibit the transcriptional activity of ATF2.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi77 – 848ATP

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. ATP-dependent 5'-3' DNA helicase activity Source: InterPro
    3. ATP-dependent DNA helicase activity Source: ProtInc
    4. chromatin DNA binding Source: UniProt
    5. damaged DNA binding Source: InterPro
    6. DNA helicase activity Source: UniProtKB
    7. identical protein binding Source: UniProtKB
    8. protein binding Source: UniProtKB
    9. RNA polymerase II core promoter sequence-specific DNA binding Source: UniProt
    10. RNA polymerase II distal enhancer sequence-specific DNA binding Source: UniProt
    11. unfolded protein binding Source: ProtInc

    GO - Biological processi

    1. ATP catabolic process Source: GOC
    2. cellular response to estradiol stimulus Source: UniProt
    3. cellular response to UV Source: UniProtKB
    4. chromatin organization Source: Reactome
    5. chromatin remodeling Source: UniProt
    6. DNA duplex unwinding Source: GOC
    7. DNA recombination Source: ProtInc
    8. DNA repair Source: ProtInc
    9. establishment of protein localization to chromatin Source: UniProt
    10. histone H2A acetylation Source: UniProtKB
    11. histone H4 acetylation Source: UniProtKB
    12. negative regulation of estrogen receptor binding Source: UniProt
    13. positive regulation of histone acetylation Source: UniProt
    14. positive regulation of transcription from RNA polymerase II promoter Source: UniProt
    15. protein folding Source: ProtInc
    16. regulation of growth Source: UniProtKB-KW
    17. transcription, DNA-templated Source: UniProtKB-KW
    18. transcriptional activation by promoter-enhancer looping Source: UniProt

    Keywords - Molecular functioni

    Activator, Chromatin regulator, Helicase, Hydrolase

    Keywords - Biological processi

    DNA damage, DNA recombination, DNA repair, Growth regulation, Transcription, Transcription regulation

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_7974. Telomere Extension By Telomerase.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RuvB-like 2 (EC:3.6.4.12)
    Alternative name(s):
    48 kDa TATA box-binding protein-interacting protein
    Short name:
    48 kDa TBP-interacting protein
    51 kDa erythrocyte cytosolic protein
    Short name:
    ECP-51
    INO80 complex subunit J
    Repressing pontin 52
    Short name:
    Reptin 52
    TIP49b
    TIP60-associated protein 54-beta
    Short name:
    TAP54-beta
    Gene namesi
    Name:RUVBL2
    Synonyms:INO80J, TIP48, TIP49B
    ORF Names:CGI-46
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:10475. RUVBL2.

    Subcellular locationi

    Nucleus matrix. Nucleusnucleoplasm. Cytoplasm. Membrane
    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.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular vesicular exosome Source: UniProt
    3. Ino80 complex Source: UniProtKB
    4. intracellular Source: LIFEdb
    5. membrane Source: UniProtKB-SubCell
    6. MLL1 complex Source: UniProtKB
    7. NuA4 histone acetyltransferase complex Source: UniProtKB
    8. nuclear euchromatin Source: UniProt
    9. nuclear matrix Source: UniProtKB-SubCell
    10. nucleoplasm Source: Reactome
    11. nucleus Source: UniProtKB
    12. ribonucleoprotein complex Source: Ensembl
    13. Swr1 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi299 – 2991D → N: Abolishes ATPase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA34888.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed4 Publications
    Chaini2 – 463462RuvB-like 2PRO_0000165644Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y230.
    PaxDbiQ9Y230.
    PeptideAtlasiQ9Y230.
    PRIDEiQ9Y230.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00009104.

    PTM databases

    PhosphoSiteiQ9Y230.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highly expressed in testis and thymus.

    Gene expression databases

    ArrayExpressiQ9Y230.
    BgeeiQ9Y230.
    CleanExiHS_RUVBL2.
    GenevestigatoriQ9Y230.

    Organism-specific databases

    HPAiCAB012432.
    HPA042880.

    Interactioni

    Subunit structurei

    Forms homohexameric rings Probable. Can form a dodecamer with RUVBL1 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. Interacts With ATF2. 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. RUVBL2 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. 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. 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. Interacts with IGHMBP2. Interacts with TELO2. Interacts with HINT1. Component of a SWR1-like complex.16 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-352939,EBI-352939
    RUVBL1Q9Y26521EBI-352939,EBI-353675
    YY1P254905EBI-352939,EBI-765538

    Protein-protein interaction databases

    BioGridi116067. 182 interactions.
    DIPiDIP-28153N.
    IntActiQ9Y230. 80 interactions.
    MINTiMINT-1136527.
    STRINGi9606.ENSP00000221413.

    Structurei

    Secondary structure

    1
    463
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni24 – 274
    Beta strandi41 – 433
    Beta strandi46 – 483
    Helixi50 – 6415
    Beta strandi72 – 787
    Helixi83 – 9412
    Beta strandi100 – 1045
    Helixi105 – 1084
    Beta strandi111 – 1133
    Helixi115 – 12511
    Beta strandi126 – 1294
    Beta strandi136 – 14813
    Beta strandi152 – 1565
    Beta strandi158 – 1647
    Beta strandi166 – 1749
    Helixi177 – 1848
    Beta strandi191 – 1966
    Turni197 – 2004
    Beta strandi201 – 2066
    Beta strandi241 – 2433
    Helixi244 – 2507
    Helixi270 – 28617
    Beta strandi290 – 2934
    Beta strandi295 – 3006
    Helixi301 – 3033
    Helixi306 – 31510
    Beta strandi323 – 3297
    Beta strandi331 – 3344
    Beta strandi341 – 3433
    Helixi348 – 3514
    Beta strandi354 – 3596
    Helixi364 – 37714
    Helixi384 – 39613
    Helixi399 – 41517
    Beta strandi419 – 4213
    Helixi423 – 43210
    Helixi436 – 4438

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2CQANMR-A132-213[»]
    2XSZX-ray3.00D/E/F2-133[»]
    D/E/F238-463[»]
    3UK6X-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-132[»]
    A/B/C/D/E/F/G/H/I/J/K/L239-463[»]
    ProteinModelPortaliQ9Y230.
    SMRiQ9Y230. Positions 24-219, 241-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y230.

    Family & Domainsi

    Domaini

    The C-terminal domain is required for association with ATF2.

    Sequence similaritiesi

    Belongs to the RuvB family.Curated

    Phylogenomic databases

    eggNOGiCOG1224.
    HOGENOMiHOG000190885.
    HOVERGENiHBG054186.
    InParanoidiQ9Y230.
    KOiK11338.
    OMAiGHKQGKL.
    OrthoDBiEOG75TMBR.
    PhylomeDBiQ9Y230.
    TreeFamiTF300469.

    Family and domain databases

    Gene3Di3.40.50.300. 3 hits.
    InterProiIPR003593. AAA+_ATPase.
    IPR004504. DNA_repair_RadA.
    IPR027417. P-loop_NTPase.
    IPR027238. RuvB-like.
    IPR010339. TIP49_C.
    [Graphical view]
    PANTHERiPTHR11093. PTHR11093. 1 hit.
    PfamiPF06068. TIP49. 1 hit.
    [Graphical view]
    PRINTSiPR01874. DNAREPAIRADA.
    SMARTiSM00382. AAA. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y230-1) [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

    MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL    50
    AARRAAGVVL EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF 100
    TAIAGSEIFS LEMSKTEALT QAFRRSIGVR IKEETEIIEG EVVEIQIDRP 150
    ATGTGSKVGK LTLKTTEMET IYDLGTKMIE SLTKDKVQAG DVITIDKATG 200
    KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH TVSLHEIDVI 250
    NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 300
    VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL 350
    LDRLLIVSTT PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR 400
    YAIQLITAAS LVCRKRKGTE VQVDDIKRVY SLFLDESRST QYMKEYQDAF 450
    LFNELKGETM DTS 463
    Length:463
    Mass (Da):51,157
    Last modified:January 23, 2007 - v3
    Checksum:i54C78E9C587D975A
    GO
    Isoform 2 (identifier: Q9Y230-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-45: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:418
    Mass (Da):46,306
    Checksum:i64C304B804D86B2E
    GO

    Sequence cautioni

    The sequence AAD34041.1 differs from that shown. Reason: Frameshift at position 401.
    The sequence AAH08355.1 differs from that shown. Reason: Frameshift at position 191.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti214 – 2141D → N in AAD34041. (PubMed:10810093)Curated
    Sequence conflicti257 – 2582FL → YV AA sequence (PubMed:10882073)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4545Missing in isoform 2. 1 PublicationVSP_056584Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y18417 mRNA. Translation: CAB46270.1.
    AB024301 mRNA. Translation: BAA76708.1.
    AF155138 mRNA. Translation: AAD38073.1.
    AF124607 mRNA. Translation: AAF87087.1.
    AF151804 mRNA. Translation: AAD34041.1. Frameshift.
    AL136743 mRNA. Translation: CAB66677.1.
    AK057498 mRNA. Translation: BAG51921.1.
    AK074542 mRNA. Translation: BAC11048.1.
    CR533507 mRNA. Translation: CAG38538.1.
    AC008687 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52426.1.
    CH471177 Genomic DNA. Translation: EAW52430.1.
    BC000428 mRNA. Translation: AAH00428.1.
    BC004531 mRNA. Translation: AAH04531.1.
    BC008355 mRNA. Translation: AAH08355.1. Frameshift.
    CCDSiCCDS42588.1.
    PIRiT46313.
    RefSeqiNP_006657.1. NM_006666.1.
    XP_005258485.1. XM_005258428.1.
    UniGeneiHs.515846.

    Genome annotation databases

    EnsembliENST00000413176; ENSP00000413890; ENSG00000183207.
    ENST00000595090; ENSP00000473172; ENSG00000183207.
    GeneIDi10856.
    KEGGihsa:10856.
    UCSCiuc002plr.1. human.

    Polymorphism databases

    DMDMi28201890.

    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
    Y18417 mRNA. Translation: CAB46270.1 .
    AB024301 mRNA. Translation: BAA76708.1 .
    AF155138 mRNA. Translation: AAD38073.1 .
    AF124607 mRNA. Translation: AAF87087.1 .
    AF151804 mRNA. Translation: AAD34041.1 . Frameshift.
    AL136743 mRNA. Translation: CAB66677.1 .
    AK057498 mRNA. Translation: BAG51921.1 .
    AK074542 mRNA. Translation: BAC11048.1 .
    CR533507 mRNA. Translation: CAG38538.1 .
    AC008687 Genomic DNA. No translation available.
    CH471177 Genomic DNA. Translation: EAW52426.1 .
    CH471177 Genomic DNA. Translation: EAW52430.1 .
    BC000428 mRNA. Translation: AAH00428.1 .
    BC004531 mRNA. Translation: AAH04531.1 .
    BC008355 mRNA. Translation: AAH08355.1 . Frameshift.
    CCDSi CCDS42588.1.
    PIRi T46313.
    RefSeqi NP_006657.1. NM_006666.1.
    XP_005258485.1. XM_005258428.1.
    UniGenei Hs.515846.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2CQA NMR - A 132-213 [» ]
    2XSZ X-ray 3.00 D/E/F 2-133 [» ]
    D/E/F 238-463 [» ]
    3UK6 X-ray 2.95 A/B/C/D/E/F/G/H/I/J/K/L 1-132 [» ]
    A/B/C/D/E/F/G/H/I/J/K/L 239-463 [» ]
    ProteinModelPortali Q9Y230.
    SMRi Q9Y230. Positions 24-219, 241-444.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116067. 182 interactions.
    DIPi DIP-28153N.
    IntActi Q9Y230. 80 interactions.
    MINTi MINT-1136527.
    STRINGi 9606.ENSP00000221413.

    Chemistry

    ChEMBLi CHEMBL2062349.

    PTM databases

    PhosphoSitei Q9Y230.

    Polymorphism databases

    DMDMi 28201890.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00009104.

    Proteomic databases

    MaxQBi Q9Y230.
    PaxDbi Q9Y230.
    PeptideAtlasi Q9Y230.
    PRIDEi Q9Y230.

    Protocols and materials databases

    DNASUi 10856.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000413176 ; ENSP00000413890 ; ENSG00000183207 .
    ENST00000595090 ; ENSP00000473172 ; ENSG00000183207 .
    GeneIDi 10856.
    KEGGi hsa:10856.
    UCSCi uc002plr.1. human.

    Organism-specific databases

    CTDi 10856.
    GeneCardsi GC19P049497.
    HGNCi HGNC:10475. RUVBL2.
    HPAi CAB012432.
    HPA042880.
    MIMi 604788. gene.
    neXtProti NX_Q9Y230.
    PharmGKBi PA34888.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1224.
    HOGENOMi HOG000190885.
    HOVERGENi HBG054186.
    InParanoidi Q9Y230.
    KOi K11338.
    OMAi GHKQGKL.
    OrthoDBi EOG75TMBR.
    PhylomeDBi Q9Y230.
    TreeFami TF300469.

    Enzyme and pathway databases

    Reactomei REACT_172610. HATs acetylate histones.
    REACT_197820. HATs acetylate histones.
    REACT_7974. Telomere Extension By Telomerase.

    Miscellaneous databases

    ChiTaRSi RUVBL2. human.
    EvolutionaryTracei Q9Y230.
    GeneWikii RUVBL2.
    GenomeRNAii 10856.
    NextBioi 41211.
    PROi Q9Y230.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y230.
    Bgeei Q9Y230.
    CleanExi HS_RUVBL2.
    Genevestigatori Q9Y230.

    Family and domain databases

    Gene3Di 3.40.50.300. 3 hits.
    InterProi IPR003593. AAA+_ATPase.
    IPR004504. DNA_repair_RadA.
    IPR027417. P-loop_NTPase.
    IPR027238. RuvB-like.
    IPR010339. TIP49_C.
    [Graphical view ]
    PANTHERi PTHR11093. PTHR11093. 1 hit.
    Pfami PF06068. TIP49. 1 hit.
    [Graphical view ]
    PRINTSi PR01874. DNAREPAIRADA.
    SMARTi SM00382. AAA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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 72-83; 131-144; 212-223; 369-372 AND 440-457.
      Tissue: Bone marrow.
    2. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, INTERACTION WITH RUVBL1.
      Tissue: Liver.
    3. "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical link to the human CGB/LHB gene cluster on chromosome 19q13.3."
      Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M., Vodovar N., Vidaud D., Vidaud M., Bieche I.
      Ann. Genet. 43:69-74(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Mammary gland.
    4. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Fetal liver.
    5. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 73-83; 116-124; 237-253 AND 254-269, INTERACTION WITH MYC.
    6. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    8. "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] (ISOFORMS 1 AND 2).
      Tissue: Embryo and Testis.
    9. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    10. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    11. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    12. "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: Colon and Lung.
    13. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-14.
      Tissue: Platelet.
    14. Bienvenut W.V., Heiserich L., Gottlieb E.
      Submitted (MAR-2008) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177; 237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Colon carcinoma.
    15. "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 30-40; 185-197; 354-365 AND 417-427, IDENTIFICATION IN THE NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    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 30-40; 72-83; 165-177; 187-197; 254-269; 354-365; 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    17. "TIP49b, a regulator of activating transcription factor 2 response to stress and DNA damage."
      Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.
      Mol. Cell. Biol. 21:8398-8413(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ATF2.
    18. "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.
    19. "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.
    20. Cited for: IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
    21. "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.
    22. "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-299, ELECTRON MICROSCOPY OF THE RUVBL1-RUVBL2 HETEROMER.
    23. "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.
    24. "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.
    25. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    26. "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.
    27. "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and ATR complexes."
      Takai H., Xie Y., de Lange T., Pavletich N.P.
      Genes Dev. 24:2019-2030(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TELO2.
    28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    29. "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.
    30. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    31. Cited for: FUNCTION, IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
    32. "Solution structure of RSGI RUH-039, a fragment of C-terminal domain of RuvB-like 2 from human cDNA."
      Mycobacterium tuberculosis structural genomics consortium (TB)
      Submitted (NOV-2005) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 132-213.

    Entry informationi

    Entry nameiRUVB2_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y230
    Secondary accession number(s): B3KQ59
    , E7ETE5, Q6FIB9, Q6PK27, Q9Y361
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2003
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 167 of the entry and version 3 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

    Keywords - Technical termi

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

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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