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Q9Y230 (RUVB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 162. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:RUVBL2
Synonyms:INO80J, TIP48, TIP49B
ORF Names:CGI-46
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length463 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.16 Ref.19 Ref.29

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.16 Ref.19 Ref.29

Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Ref.16 Ref.19 Ref.29

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. Ref.16 Ref.19 Ref.29

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

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. Ref.2 Ref.5 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.24 Ref.25 Ref.27 Ref.29

Subcellular location

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.

Tissue specificity

Ubiquitously expressed. Highly expressed in testis and thymus.

Domain

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

Sequence similarities

Belongs to the RuvB family.

Sequence caution

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.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Growth regulation
Transcription
Transcription regulation
   Cellular componentCytoplasm
Membrane
Nucleus
   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_processATP catabolic process

Inferred from direct assay Ref.13. Source: GOC

DNA duplex unwinding

Inferred from direct assay Ref.1. Source: GOC

DNA recombination

Traceable author statement Ref.2. Source: ProtInc

DNA repair

Traceable author statement Ref.2. Source: ProtInc

cellular response to UV

Inferred from mutant phenotype Ref.21. Source: UniProtKB

chromatin organization

Traceable author statement. Source: Reactome

histone H2A acetylation

Inferred from direct assay Ref.16. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.16. Source: UniProtKB

protein folding

Traceable author statement Ref.1. Source: ProtInc

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentIno80 complex

Inferred from direct assay Ref.21Ref.27. Source: UniProtKB

MLL1 complex

Inferred from direct assay Ref.17. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from direct assay Ref.13Ref.16. Source: UniProtKB

Swr1 complex

Inferred from direct assay Ref.29. Source: UniProtKB

cytoplasm

Inferred from direct assay. Source: HPA

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

intracellular

Inferred from direct assay. Source: LIFEdb

membrane

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.1Ref.21. Source: UniProtKB

ribonucleoprotein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent 5'-3' DNA helicase activity

Inferred from electronic annotation. Source: InterPro

ATP-dependent DNA helicase activity

Traceable author statement Ref.2. Source: ProtInc

DNA helicase activity

Inferred from direct assay Ref.1. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

identical protein binding

Inferred from direct assay Ref.13. Source: UniProtKB

unfolded protein binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11 Ref.12
Chain2 – 463462RuvB-like 2
PRO_0000165644

Regions

Nucleotide binding77 – 848ATP

Amino acid modifications

Modified residue21N-acetylalanine Ref.12 Ref.23 Ref.28

Experimental info

Mutagenesis2991D → N: Abolishes ATPase activity. Ref.20
Sequence conflict2141D → N in AAD34041. Ref.6
Sequence conflict257 – 2582FL → YV AA sequence Ref.5

Secondary structure

..................................................................... 463
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9Y230 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 54C78E9C587D975A

FASTA46351,157
        10         20         30         40         50         60 
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL 

        70         80         90        100        110        120 
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT 

       130        140        150        160        170        180 
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE 

       190        200        210        220        230        240 
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH 

       250        260        270        280        290        300 
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE 

       310        320        330        340        350        360 
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT 

       370        380        390        400        410        420 
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE 

       430        440        450        460 
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS 

« Hide

References

« Hide 'large scale' references
[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], 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], 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].
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].
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], 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].
[7]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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. 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].
Tissue: Embryo.
[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].
[10]"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].
Tissue: Colon and Lung.
[11]"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.
[12]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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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 INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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].
[24]"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.
[25]"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.
[26]"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].
[27]"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.
[28]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"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.
[30]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AK074542 mRNA. Translation: BAC11048.1.
CR533507 mRNA. Translation: CAG38538.1.
BC000428 mRNA. Translation: AAH00428.1.
BC004531 mRNA. Translation: AAH04531.1.
BC008355 mRNA. Translation: AAH08355.1. Frameshift.
PIRT46313.
RefSeqNP_006657.1. NM_006666.1.
UniGeneHs.515846.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQANMR-A132-212[»]
2XSZX-ray3.00D/E/F2-463[»]
3UK6X-ray2.95A/B/C/D/E/F/G/H/I/J/K/L1-463[»]
ProteinModelPortalQ9Y230.
SMRQ9Y230. Positions 24-219, 241-444.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116067. 184 interactions.
DIPDIP-28153N.
IntActQ9Y230. 79 interactions.
MINTMINT-1136527.
STRING9606.ENSP00000221413.

Chemistry

ChEMBLCHEMBL2062349.

PTM databases

PhosphoSiteQ9Y230.

Polymorphism databases

DMDM28201890.

2D gel databases

REPRODUCTION-2DPAGEIPI00009104.

Proteomic databases

PaxDbQ9Y230.
PeptideAtlasQ9Y230.
PRIDEQ9Y230.

Protocols and materials databases

DNASU10856.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000595090; ENSP00000473172; ENSG00000183207.
GeneID10856.
KEGGhsa:10856.
UCSCuc002plr.1. human.

Organism-specific databases

CTD10856.
GeneCardsGC19P049497.
HGNCHGNC:10475. RUVBL2.
HPACAB012432.
HPA042880.
MIM604788. gene.
neXtProtNX_Q9Y230.
PharmGKBPA34888.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1224.
HOGENOMHOG000190885.
HOVERGENHBG054186.
InParanoidQ9Y230.
KOK11338.
OMAKTSLRYA.
OrthoDBEOG75TMBR.
PhylomeDBQ9Y230.
TreeFamTF300469.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.

Gene expression databases

ArrayExpressQ9Y230.
BgeeQ9Y230.
CleanExHS_RUVBL2.
GenevestigatorQ9Y230.

Family and domain databases

Gene3D3.40.50.300. 3 hits.
InterProIPR003593. AAA+_ATPase.
IPR004504. DNA_repair_RadA.
IPR027417. P-loop_NTPase.
IPR027238. RuvB-like.
IPR010339. TIP49_C.
[Graphical view]
PANTHERPTHR11093. PTHR11093. 1 hit.
PfamPF06068. TIP49. 1 hit.
[Graphical view]
PRINTSPR01874. DNAREPAIRADA.
SMARTSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSRUVBL2. human.
EvolutionaryTraceQ9Y230.
GeneWikiRUVBL2.
GenomeRNAi10856.
NextBio41211.
PROQ9Y230.
SOURCESearch...

Entry information

Entry nameRUVB2_HUMAN
AccessionPrimary (citable) accession number: Q9Y230
Secondary accession number(s): Q6FIB9, Q6PK27, Q9Y361
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2003
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 162 of the entry and version 3 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 19

Human chromosome 19: entries, gene names and cross-references to MIM