Full text data of RUVBL2
RUVBL2
(INO80J, TIP48, TIP49B)
[Confidence: high (present in two of the MS resources)]
RuvB-like 2; 3.6.4.12 (48 kDa TATA box-binding protein-interacting protein; 48 kDa TBP-interacting protein; 51 kDa erythrocyte cytosolic protein; ECP-51; INO80 complex subunit J; Repressing pontin 52; Reptin 52; TIP49b; TIP60-associated protein 54-beta; TAP54-beta)
RuvB-like 2; 3.6.4.12 (48 kDa TATA box-binding protein-interacting protein; 48 kDa TBP-interacting protein; 51 kDa erythrocyte cytosolic protein; ECP-51; INO80 complex subunit J; Repressing pontin 52; Reptin 52; TIP49b; TIP60-associated protein 54-beta; TAP54-beta)
hRBCD
IPI00009104
IPI00009104 Similar to Erythrocyte cytosolic protein of 51 kDa, EC bone marrow, ubiquitous, Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 188 kDa
IPI00009104 Similar to Erythrocyte cytosolic protein of 51 kDa, EC bone marrow, ubiquitous, Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histone H4 and H2A soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nuclear n/a expected molecular weight found in band found in band around 188 kDa
UniProt
Q9Y230
ID RUVB2_HUMAN Reviewed; 463 AA.
AC Q9Y230; Q6FIB9; Q6PK27; Q9Y361;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12;
DE AltName: Full=48 kDa TATA box-binding protein-interacting protein;
DE Short=48 kDa TBP-interacting protein;
DE AltName: Full=51 kDa erythrocyte cytosolic protein;
DE Short=ECP-51;
DE AltName: Full=INO80 complex subunit J;
DE AltName: Full=Repressing pontin 52;
DE Short=Reptin 52;
DE AltName: Full=TIP49b;
DE AltName: Full=TIP60-associated protein 54-beta;
DE Short=TAP54-beta;
GN Name=RUVBL2; Synonyms=INO80J, TIP48, TIP49B; ORFNames=CGI-46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-83; 131-144;
RP 212-223; 369-372 AND 440-457.
RC TISSUE=Bone marrow;
RX PubMed=10524211; DOI=10.1016/S0167-4781(99)00104-9;
RA Salzer U., Kubicek M., Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid
RT cytosolic proteins.";
RL Biochim. Biophys. Acta 1446:365-370(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH
RP RUVBL1.
RC TISSUE=Liver;
RX PubMed=10428817; DOI=10.1074/jbc.274.32.22437;
RA Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A.,
RA Okazaki K., Morishita T., Tamura T.-A.;
RT "TIP49b, a new RuvB-like DNA helicase, is included in a complex
RT together with another RuvB-like DNA helicase, TIP49a.";
RL J. Biol. Chem. 274:22437-22444(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=10998447; DOI=10.1016/S0003-3995(00)01016-9;
RA Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M.,
RA Vodovar N., Vidaud D., Vidaud M., Bieche I.;
RT "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern,
RT physical link to the human CGB/LHB gene cluster on chromosome
RT 19q13.3.";
RL Ann. Genet. 43:69-74(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=11080158; DOI=10.1093/emboj/19.22.6121;
RA Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U.,
RA Aragnol D., Kemler R., Pradel J.;
RT "Pontin52 and reptin52 function as antagonistic regulators of beta-
RT catenin signalling activity.";
RL EMBO J. 19:6121-6130(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-83; 116-124;
RP 237-253 AND 254-269, AND INTERACTION WITH MYC.
RX PubMed=10882073; DOI=10.1016/S1097-2765(00)80427-X;
RA Wood M.A., McMahon S.B., Cole M.D.;
RT "An ATPase/helicase complex is an essential cofactor for oncogenic
RT transformation by c-Myc.";
RL Mol. Cell 5:321-330(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177;
RP 237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427,
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=10966108; DOI=10.1016/S0092-8674(00)00051-9;
RA Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J.,
RA Horikoshi M., Scully R., Qin J., Nakatani Y.;
RT "Involvement of the TIP60 histone acetylase complex in DNA repair and
RT apoptosis.";
RL Cell 102:463-473(2000).
RN [14]
RP PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365;
RP 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, AND MASS
RP SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.C300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian
RT TRRAP/TIP60-containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [15]
RP INTERACTION WITH ATF2.
RX PubMed=11713276; DOI=10.1128/MCB.21.24.8398-8413.2001;
RA Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.;
RT "TIP49b, a regulator of activating transcription factor 2 response to
RT stress and DNA damage.";
RL Mol. Cell. Biol. 21:8398-8413(2001).
RN [16]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING
RP COMPLEX.
RX PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [17]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [18]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.M509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the
RT yeast INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [19]
RP INTERACTION WITH HINT1, AND FUNCTION.
RX PubMed=16014379; DOI=10.1242/jcs.02437;
RA Weiske J., Huber O.;
RT "The histidine triad protein Hint1 interacts with Pontin and Reptin
RT and inhibits TCF-beta-catenin-mediated transcription.";
RL J. Cell Sci. 118:3117-3129(2005).
RN [20]
RP SUBUNIT, MUTAGENESIS OF ASP-299, AND ELECTRON MICROSCOPY OF THE
RP RUVBL1-RUVBL2 HETEROMER.
RX PubMed=17157868; DOI=10.1016/j.jmb.2006.11.030;
RA Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.;
RT "Dodecameric structure and ATPase activity of the human TIP48/TIP49
RT complex.";
RL J. Mol. Biol. 366:179-192(2007).
RN [21]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND PROTEIN INTERACTION.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NPAT.
RX PubMed=17967892; DOI=10.1128/MCB.00607-07;
RA DeRan M., Pulvino M., Greene E., Su C., Zhao J.;
RT "Transcriptional activation of histone genes requires NPAT-dependent
RT recruitment of TRRAP-Tip60 complex to histone promoters during the
RT G1/S phase transition.";
RL Mol. Cell. Biol. 28:435-447(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP INTERACTION WITH IGHMBP2.
RX PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA Mourelatos Z.;
RT "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT translational machinery.";
RL Hum. Mol. Genet. 18:2115-2126(2009).
RN [25]
RP INTERACTION WITH TELO2.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR
RT and ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.M111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex:
RT An evolutionarily conserved core complex catalyzes ATP-dependent
RT nucleosome remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP STRUCTURE BY NMR OF 132-213.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Solution structure of RSGI RUH-039, a fragment of C-terminal domain
RT of RuvB-like 2 from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (5' to 3') activity; hexamerization is
CC thought to be critical for ATP hydrolysis and adjacent subunits in
CC the ring-like structure contribute to the ATPase activity.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
CC which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A.
CC This modification may both alter nucleosome - DNA interactions and
CC promote interaction of the modified histones with other proteins
CC which positively regulate transcription. This complex may be
CC required for the activation of transcriptional programs associated
CC with oncogene and proto-oncogene mediated growth induction, tumor
CC suppressor mediated growth arrest and replicative senescence,
CC apoptosis, and DNA repair. The NuA4 complex ATPase and helicase
CC activities seem to be, at least in part, contributed by the
CC association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a
CC direct role in DNA repair when recruited to sites of DNA damage.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair.
CC -!- FUNCTION: Plays an essential role in oncogenic transformation by
CC MYC and also modulates transcriptional activation by the
CC LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional
CC activity of ATF2.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a
CC dodecamer with RUVBL1 made of two stacked hexameric rings;
CC however, even though RUVBL1 and RUVBL2 are present in equimolar
CC ratio, the oligomeric status of each hexamer is not known.
CC Oligomerization may regulate binding to nucleic acids and
CC conversely, binding to nucleic acids may affect the dodecameric
CC assembly. Interacts with the transcriptional activation domain of
CC MYC. Interacts With ATF2. Component of the RNA polymerase II
CC holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1
CC complex and TBP. Component of the NuA4 histone acetyltransferase
CC complex which contains the catalytic subunit KAT5/TIP60 and the
CC subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4
CC complex interacts with MYC and the adenovirus E1A protein. RUVBL2
CC interacts with EP400. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72
CC and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin-
CC remodeling INO80 complex; specifically part of a complex module
CC associated with the helicase ATP-binding and the helicase C-
CC terminal domain of INO80. Component of some MLL1/MLL complex, at
CC least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
CC MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with
CC IGHMBP2. Interacts with TELO2. Interacts with HINT1.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-352939, EBI-352939;
CC Q9Y265:RUVBL1; NbExp=21; IntAct=EBI-352939, EBI-353675;
CC P25490:YY1; NbExp=5; IntAct=EBI-352939, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
CC Cytoplasm. Membrane. Note=Mainly localized in the nucleus,
CC associated with nuclear matrix or in the nuclear cytosol. Although
CC it is also present in the cytoplasm and associated with the cell
CC membranes.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC testis and thymus.
CC -!- DOMAIN: The C-terminal domain is required for association with
CC ATF2.
CC -!- SIMILARITY: Belongs to the RuvB family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34041.1; Type=Frameshift; Positions=401;
CC Sequence=AAH08355.1; Type=Frameshift; Positions=191;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL2ID42185ch19q13.html";
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DR EMBL; Y18417; CAB46270.1; -; mRNA.
DR EMBL; AB024301; BAA76708.1; -; mRNA.
DR EMBL; AF155138; AAD38073.1; -; mRNA.
DR EMBL; AF124607; AAF87087.1; -; mRNA.
DR EMBL; AF151804; AAD34041.1; ALT_FRAME; mRNA.
DR EMBL; AL136743; CAB66677.1; -; mRNA.
DR EMBL; AK074542; BAC11048.1; -; mRNA.
DR EMBL; CR533507; CAG38538.1; -; mRNA.
DR EMBL; BC000428; AAH00428.1; -; mRNA.
DR EMBL; BC004531; AAH04531.1; -; mRNA.
DR EMBL; BC008355; AAH08355.1; ALT_FRAME; mRNA.
DR PIR; T46313; T46313.
DR RefSeq; NP_006657.1; NM_006666.1.
DR UniGene; Hs.515846; -.
DR PDB; 2CQA; NMR; -; A=132-212.
DR PDB; 2XSZ; X-ray; 3.00 A; D/E/F=2-463.
DR PDB; 3UK6; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-463.
DR PDBsum; 2CQA; -.
DR PDBsum; 2XSZ; -.
DR PDBsum; 3UK6; -.
DR ProteinModelPortal; Q9Y230; -.
DR SMR; Q9Y230; 24-219, 241-444.
DR DIP; DIP-28153N; -.
DR IntAct; Q9Y230; 77.
DR MINT; MINT-1136527; -.
DR STRING; 9606.ENSP00000221413; -.
DR ChEMBL; CHEMBL2062349; -.
DR PhosphoSite; Q9Y230; -.
DR DMDM; 28201890; -.
DR REPRODUCTION-2DPAGE; IPI00009104; -.
DR PaxDb; Q9Y230; -.
DR PeptideAtlas; Q9Y230; -.
DR PRIDE; Q9Y230; -.
DR DNASU; 10856; -.
DR Ensembl; ENST00000595090; ENSP00000473172; ENSG00000183207.
DR GeneID; 10856; -.
DR KEGG; hsa:10856; -.
DR UCSC; uc002plr.1; human.
DR CTD; 10856; -.
DR GeneCards; GC19P049497; -.
DR HGNC; HGNC:10475; RUVBL2.
DR HPA; CAB012432; -.
DR MIM; 604788; gene.
DR neXtProt; NX_Q9Y230; -.
DR PharmGKB; PA34888; -.
DR eggNOG; COG1224; -.
DR HOGENOM; HOG000190885; -.
DR HOVERGEN; HBG054186; -.
DR InParanoid; Q9Y230; -.
DR KO; K11338; -.
DR OMA; KTSLRYA; -.
DR OrthoDB; EOG75TMBR; -.
DR ChiTaRS; RUVBL2; human.
DR EvolutionaryTrace; Q9Y230; -.
DR GeneWiki; RUVBL2; -.
DR GenomeRNAi; 10856; -.
DR NextBio; 41211; -.
DR PRO; PR:Q9Y230; -.
DR ArrayExpress; Q9Y230; -.
DR Bgee; Q9Y230; -.
DR CleanEx; HS_RUVBL2; -.
DR Genevestigator; Q9Y230; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR010339; TIP49_C.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR Pfam; PF06068; TIP49; 1.
DR PRINTS; PR01874; DNAREPAIRADA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; ATP-binding;
KW Chromatin regulator; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Growth regulation; Helicase; Hydrolase; Membrane; Nucleotide-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 463 RuvB-like 2.
FT /FTId=PRO_0000165644.
FT NP_BIND 77 84 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MUTAGEN 299 299 D->N: Abolishes ATPase activity.
FT CONFLICT 214 214 D -> N (in Ref. 6; AAD34041).
FT CONFLICT 257 258 FL -> YV (in Ref. 5; AA sequence).
FT TURN 24 27
FT STRAND 41 43
FT STRAND 46 48
FT HELIX 50 64
FT STRAND 72 78
FT HELIX 83 94
FT STRAND 100 104
FT HELIX 105 108
FT STRAND 111 113
FT HELIX 115 125
FT STRAND 126 129
FT STRAND 136 148
FT STRAND 152 156
FT STRAND 158 164
FT STRAND 166 174
FT HELIX 177 184
FT STRAND 191 196
FT TURN 197 200
FT STRAND 201 206
FT STRAND 241 243
FT HELIX 244 250
FT HELIX 270 286
FT STRAND 290 293
FT STRAND 295 300
FT HELIX 301 303
FT HELIX 306 315
FT STRAND 323 329
FT STRAND 331 334
FT STRAND 341 343
FT HELIX 348 351
FT STRAND 354 359
FT HELIX 364 377
FT HELIX 384 396
FT HELIX 399 415
FT STRAND 419 421
FT HELIX 423 432
FT HELIX 436 443
SQ SEQUENCE 463 AA; 51157 MW; 54C78E9C587D975A CRC64;
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS
//
ID RUVB2_HUMAN Reviewed; 463 AA.
AC Q9Y230; Q6FIB9; Q6PK27; Q9Y361;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 159.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12;
DE AltName: Full=48 kDa TATA box-binding protein-interacting protein;
DE Short=48 kDa TBP-interacting protein;
DE AltName: Full=51 kDa erythrocyte cytosolic protein;
DE Short=ECP-51;
DE AltName: Full=INO80 complex subunit J;
DE AltName: Full=Repressing pontin 52;
DE Short=Reptin 52;
DE AltName: Full=TIP49b;
DE AltName: Full=TIP60-associated protein 54-beta;
DE Short=TAP54-beta;
GN Name=RUVBL2; Synonyms=INO80J, TIP48, TIP49B; ORFNames=CGI-46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 72-83; 131-144;
RP 212-223; 369-372 AND 440-457.
RC TISSUE=Bone marrow;
RX PubMed=10524211; DOI=10.1016/S0167-4781(99)00104-9;
RA Salzer U., Kubicek M., Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression
RT of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid
RT cytosolic proteins.";
RL Biochim. Biophys. Acta 1446:365-370(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND INTERACTION WITH
RP RUVBL1.
RC TISSUE=Liver;
RX PubMed=10428817; DOI=10.1074/jbc.274.32.22437;
RA Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A.,
RA Okazaki K., Morishita T., Tamura T.-A.;
RT "TIP49b, a new RuvB-like DNA helicase, is included in a complex
RT together with another RuvB-like DNA helicase, TIP49a.";
RL J. Biol. Chem. 274:22437-22444(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Mammary gland;
RX PubMed=10998447; DOI=10.1016/S0003-3995(00)01016-9;
RA Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M.,
RA Vodovar N., Vidaud D., Vidaud M., Bieche I.;
RT "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern,
RT physical link to the human CGB/LHB gene cluster on chromosome
RT 19q13.3.";
RL Ann. Genet. 43:69-74(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal liver;
RX PubMed=11080158; DOI=10.1093/emboj/19.22.6121;
RA Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U.,
RA Aragnol D., Kemler R., Pradel J.;
RT "Pontin52 and reptin52 function as antagonistic regulators of beta-
RT catenin signalling activity.";
RL EMBO J. 19:6121-6130(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 73-83; 116-124;
RP 237-253 AND 254-269, AND INTERACTION WITH MYC.
RX PubMed=10882073; DOI=10.1016/S1097-2765(00)80427-X;
RA Wood M.A., McMahon S.B., Cole M.D.;
RT "An ATPase/helicase complex is an essential cofactor for oncogenic
RT transformation by c-Myc.";
RL Mol. Cell 5:321-330(2000).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.GR1547R;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [11]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [12]
RP PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177;
RP 237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT ALA-2, AND MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [13]
RP PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427,
RP IDENTIFICATION IN THE NUA4 COMPLEX, AND MASS SPECTROMETRY.
RX PubMed=10966108; DOI=10.1016/S0092-8674(00)00051-9;
RA Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J.,
RA Horikoshi M., Scully R., Qin J., Nakatani Y.;
RT "Involvement of the TIP60 histone acetylase complex in DNA repair and
RT apoptosis.";
RL Cell 102:463-473(2000).
RN [14]
RP PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365;
RP 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, AND MASS
RP SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.C300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian
RT TRRAP/TIP60-containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [15]
RP INTERACTION WITH ATF2.
RX PubMed=11713276; DOI=10.1128/MCB.21.24.8398-8413.2001;
RA Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.;
RT "TIP49b, a regulator of activating transcription factor 2 response to
RT stress and DNA damage.";
RL Mol. Cell. Biol. 21:8398-8413(2001).
RN [16]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING
RP COMPLEX.
RX PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [17]
RP IDENTIFICATION IN THE MLL1/MLL COMPLEX.
RX PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
RA Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
RA Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
RT "Physical association and coordinate function of the H3 K4
RT methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
RL Cell 121:873-885(2005).
RN [18]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.M509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A.,
RA Washburn M.P., Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the
RT yeast INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [19]
RP INTERACTION WITH HINT1, AND FUNCTION.
RX PubMed=16014379; DOI=10.1242/jcs.02437;
RA Weiske J., Huber O.;
RT "The histidine triad protein Hint1 interacts with Pontin and Reptin
RT and inhibits TCF-beta-catenin-mediated transcription.";
RL J. Cell Sci. 118:3117-3129(2005).
RN [20]
RP SUBUNIT, MUTAGENESIS OF ASP-299, AND ELECTRON MICROSCOPY OF THE
RP RUVBL1-RUVBL2 HETEROMER.
RX PubMed=17157868; DOI=10.1016/j.jmb.2006.11.030;
RA Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.;
RT "Dodecameric structure and ATPase activity of the human TIP48/TIP49
RT complex.";
RL J. Mol. Biol. 366:179-192(2007).
RN [21]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND PROTEIN INTERACTION.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [22]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NPAT.
RX PubMed=17967892; DOI=10.1128/MCB.00607-07;
RA DeRan M., Pulvino M., Greene E., Su C., Zhao J.;
RT "Transcriptional activation of histone genes requires NPAT-dependent
RT recruitment of TRRAP-Tip60 complex to histone promoters during the
RT G1/S phase transition.";
RL Mol. Cell. Biol. 28:435-447(2008).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [24]
RP INTERACTION WITH IGHMBP2.
RX PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA Mourelatos Z.;
RT "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT translational machinery.";
RL Hum. Mol. Genet. 18:2115-2126(2009).
RN [25]
RP INTERACTION WITH TELO2.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR
RT and ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [27]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.M111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex:
RT An evolutionarily conserved core complex catalyzes ATP-dependent
RT nucleosome remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [28]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [29]
RP STRUCTURE BY NMR OF 132-213.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Solution structure of RSGI RUH-039, a fragment of C-terminal domain
RT of RuvB-like 2 from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (5' to 3') activity; hexamerization is
CC thought to be critical for ATP hydrolysis and adjacent subunits in
CC the ring-like structure contribute to the ATPase activity.
CC -!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
CC which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A.
CC This modification may both alter nucleosome - DNA interactions and
CC promote interaction of the modified histones with other proteins
CC which positively regulate transcription. This complex may be
CC required for the activation of transcriptional programs associated
CC with oncogene and proto-oncogene mediated growth induction, tumor
CC suppressor mediated growth arrest and replicative senescence,
CC apoptosis, and DNA repair. The NuA4 complex ATPase and helicase
CC activities seem to be, at least in part, contributed by the
CC association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a
CC direct role in DNA repair when recruited to sites of DNA damage.
CC -!- FUNCTION: Proposed core component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair.
CC -!- FUNCTION: Plays an essential role in oncogenic transformation by
CC MYC and also modulates transcriptional activation by the
CC LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional
CC activity of ATF2.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Forms homohexameric rings (Probable). Can form a
CC dodecamer with RUVBL1 made of two stacked hexameric rings;
CC however, even though RUVBL1 and RUVBL2 are present in equimolar
CC ratio, the oligomeric status of each hexamer is not known.
CC Oligomerization may regulate binding to nucleic acids and
CC conversely, binding to nucleic acids may affect the dodecameric
CC assembly. Interacts with the transcriptional activation domain of
CC MYC. Interacts With ATF2. Component of the RNA polymerase II
CC holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1
CC complex and TBP. Component of the NuA4 histone acetyltransferase
CC complex which contains the catalytic subunit KAT5/TIP60 and the
CC subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
CC MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4
CC complex interacts with MYC and the adenovirus E1A protein. RUVBL2
CC interacts with EP400. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72
CC and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin-
CC remodeling INO80 complex; specifically part of a complex module
CC associated with the helicase ATP-binding and the helicase C-
CC terminal domain of INO80. Component of some MLL1/MLL complex, at
CC least composed of the core components KMT2A/MLL1, ASH2L,
CC HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
CC BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
CC MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
CC SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with
CC IGHMBP2. Interacts with TELO2. Interacts with HINT1.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-352939, EBI-352939;
CC Q9Y265:RUVBL1; NbExp=21; IntAct=EBI-352939, EBI-353675;
CC P25490:YY1; NbExp=5; IntAct=EBI-352939, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
CC Cytoplasm. Membrane. Note=Mainly localized in the nucleus,
CC associated with nuclear matrix or in the nuclear cytosol. Although
CC it is also present in the cytoplasm and associated with the cell
CC membranes.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC testis and thymus.
CC -!- DOMAIN: The C-terminal domain is required for association with
CC ATF2.
CC -!- SIMILARITY: Belongs to the RuvB family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34041.1; Type=Frameshift; Positions=401;
CC Sequence=AAH08355.1; Type=Frameshift; Positions=191;
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL2ID42185ch19q13.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
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DR EMBL; Y18417; CAB46270.1; -; mRNA.
DR EMBL; AB024301; BAA76708.1; -; mRNA.
DR EMBL; AF155138; AAD38073.1; -; mRNA.
DR EMBL; AF124607; AAF87087.1; -; mRNA.
DR EMBL; AF151804; AAD34041.1; ALT_FRAME; mRNA.
DR EMBL; AL136743; CAB66677.1; -; mRNA.
DR EMBL; AK074542; BAC11048.1; -; mRNA.
DR EMBL; CR533507; CAG38538.1; -; mRNA.
DR EMBL; BC000428; AAH00428.1; -; mRNA.
DR EMBL; BC004531; AAH04531.1; -; mRNA.
DR EMBL; BC008355; AAH08355.1; ALT_FRAME; mRNA.
DR PIR; T46313; T46313.
DR RefSeq; NP_006657.1; NM_006666.1.
DR UniGene; Hs.515846; -.
DR PDB; 2CQA; NMR; -; A=132-212.
DR PDB; 2XSZ; X-ray; 3.00 A; D/E/F=2-463.
DR PDB; 3UK6; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-463.
DR PDBsum; 2CQA; -.
DR PDBsum; 2XSZ; -.
DR PDBsum; 3UK6; -.
DR ProteinModelPortal; Q9Y230; -.
DR SMR; Q9Y230; 24-219, 241-444.
DR DIP; DIP-28153N; -.
DR IntAct; Q9Y230; 77.
DR MINT; MINT-1136527; -.
DR STRING; 9606.ENSP00000221413; -.
DR ChEMBL; CHEMBL2062349; -.
DR PhosphoSite; Q9Y230; -.
DR DMDM; 28201890; -.
DR REPRODUCTION-2DPAGE; IPI00009104; -.
DR PaxDb; Q9Y230; -.
DR PeptideAtlas; Q9Y230; -.
DR PRIDE; Q9Y230; -.
DR DNASU; 10856; -.
DR Ensembl; ENST00000595090; ENSP00000473172; ENSG00000183207.
DR GeneID; 10856; -.
DR KEGG; hsa:10856; -.
DR UCSC; uc002plr.1; human.
DR CTD; 10856; -.
DR GeneCards; GC19P049497; -.
DR HGNC; HGNC:10475; RUVBL2.
DR HPA; CAB012432; -.
DR MIM; 604788; gene.
DR neXtProt; NX_Q9Y230; -.
DR PharmGKB; PA34888; -.
DR eggNOG; COG1224; -.
DR HOGENOM; HOG000190885; -.
DR HOVERGEN; HBG054186; -.
DR InParanoid; Q9Y230; -.
DR KO; K11338; -.
DR OMA; KTSLRYA; -.
DR OrthoDB; EOG75TMBR; -.
DR ChiTaRS; RUVBL2; human.
DR EvolutionaryTrace; Q9Y230; -.
DR GeneWiki; RUVBL2; -.
DR GenomeRNAi; 10856; -.
DR NextBio; 41211; -.
DR PRO; PR:Q9Y230; -.
DR ArrayExpress; Q9Y230; -.
DR Bgee; Q9Y230; -.
DR CleanEx; HS_RUVBL2; -.
DR Genevestigator; Q9Y230; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0030529; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR010339; TIP49_C.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR Pfam; PF06068; TIP49; 1.
DR PRINTS; PR01874; DNAREPAIRADA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; ATP-binding;
KW Chromatin regulator; Complete proteome; Cytoplasm;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Growth regulation; Helicase; Hydrolase; Membrane; Nucleotide-binding;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 463 RuvB-like 2.
FT /FTId=PRO_0000165644.
FT NP_BIND 77 84 ATP.
FT MOD_RES 2 2 N-acetylalanine.
FT MUTAGEN 299 299 D->N: Abolishes ATPase activity.
FT CONFLICT 214 214 D -> N (in Ref. 6; AAD34041).
FT CONFLICT 257 258 FL -> YV (in Ref. 5; AA sequence).
FT TURN 24 27
FT STRAND 41 43
FT STRAND 46 48
FT HELIX 50 64
FT STRAND 72 78
FT HELIX 83 94
FT STRAND 100 104
FT HELIX 105 108
FT STRAND 111 113
FT HELIX 115 125
FT STRAND 126 129
FT STRAND 136 148
FT STRAND 152 156
FT STRAND 158 164
FT STRAND 166 174
FT HELIX 177 184
FT STRAND 191 196
FT TURN 197 200
FT STRAND 201 206
FT STRAND 241 243
FT HELIX 244 250
FT HELIX 270 286
FT STRAND 290 293
FT STRAND 295 300
FT HELIX 301 303
FT HELIX 306 315
FT STRAND 323 329
FT STRAND 331 334
FT STRAND 341 343
FT HELIX 348 351
FT STRAND 354 359
FT HELIX 364 377
FT HELIX 384 396
FT HELIX 399 415
FT STRAND 419 421
FT HELIX 423 432
FT HELIX 436 443
SQ SEQUENCE 463 AA; 51157 MW; 54C78E9C587D975A CRC64;
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS
//
MIM
604788
*RECORD*
*FIELD* NO
604788
*FIELD* TI
*604788 RUVB, E. COLI, HOMOLOG-LIKE 2; RUVBL2
;;TATA BOX-BINDING PROTEIN-INTERACTING PROTEIN, 48-KD; TIP48;;
read moreTBP-INTERACTING PROTEIN, 48-KD;;
TIP49B;;
REPTIN;;
ERYTHROCYTE CYTOSOLIC PROTEIN, 51-KD; ECP51
*FIELD* TX
CLONING
Most organisms contain multiple DNA helicases that catalyze the
unwinding of double-stranded DNA to single-stranded DNA in an
ATP-dependent manner, an essential process in replication, repair, and
transcription. RuvB is a bacterial DNA helicase involved in homologous
recombination and double-strand break repair. By amplifying sequences
related to 2 EST clones, Kanemaki et al. (1999) obtained a cDNA encoding
RuvB-like-2 (RUVBL2), which they termed TIP49B. The deduced 463-amino
acid protein contains Walker A and B motifs and is highly similar
structurally to other TIP49 family proteins, including TIP49A (RUVBL1;
603449). Western blot analysis revealed that, similar to RUVBL1, RUVBL2
is ubiquitously expressed, with highest levels in testis and thymus.
Using affinity chromatography of erythrocyte cytosol, followed by
micropeptide sequence analysis, EST database searching, PCR, and RACE,
Salzer et al. (1999) isolated cDNAs encoding RUVBL1 and RUVBL2, which
they termed ECP54 and ECP51, respectively. Northern blot analysis
revealed wide expression of a 1.5-kb RUVBL2 transcript that was most
abundant in heart, skeletal muscle, and testis.
Wood et al. (2000) identified human homologs of the RuvB protein. By use
of the MYC (190080) transactivation domain to affinity purify tightly
associated nuclear proteins, they identified RUVBL1 and RUVBL2, which
they called TIP48. RUVBL1 and RUVBL2 are both highly conserved in
evolution and contain ATPase/helicase motifs. The RUVBL2 protein
contains 463 amino acids and shares 45% amino acid identity with RUVBL1.
By RT-PCR, Parfait et al. (2000) found that RUVBL2, like RUVBL1, is
ubiquitously expressed in human tissues, with highest expression in
testis.
GENE FUNCTION
Functional analysis by Kanemaki et al. (1999) showed that RUVBL2 has
both ATPase and DNA helicase (preferentially moving in the 5-prime to
3-prime direction) activity and that RUVBL2 binds to RUVBL1.
Coimmunoprecipitation assays determined that RUVBL1 and RUVBL2 are
included in an approximately 700-kD complex in the cell nucleus. Gene
disruption analysis showed that like RUVBL1, RUVBL2 is an essential gene
for growth in yeast.
Wood et al. (2000) found that RUVBL1 and RUVBL2 are complexed with MYC
in vivo, and binding is dependent on a MYC domain essential for
oncogenic activity.
The NuA4 histone acetyltransferase (HAT) complex is responsible for
acetylation of the N-terminal tails of histone H4 (see 602822) and H2A
(see 613499) in yeast. Its catalytic subunit, Esa1, is homologous to
human TIP60 (HTATIP; 601409). Using affinity purification, Western blot
analysis, cell fractionation, immunoprecipitation, and mass
spectrometry, Doyon et al. (2004) found that TIP60 and its splice
variant, TIP60B/PLIP, were part of a multisubunit NuA4 complex with HAT
activity in several human cell lines. They identified RUVBL2 as 1 of 3
subunits specific to the human NuA4 HAT complex.
Using RNA interference in mouse embryonic stem (ES) cells, Fazzio et al.
(2008) found that depletion of any of 7 components of the Tip60-p400
(EP400; 606265) HAT and nucleosome remodeling complex, including Ruvbl2,
caused the same phenotype. Unlike normal ES cells, which grow in
spherical 3-dimensional colonies, ES cells depleted of any the 7
Tip60-p400 HAT components showed a flattened and elongated morphology,
with monolayer growth and reduced cell-cell contacts. These knockdown
cells continued to cycle, with reduced cells in S phase and increased
cells in G2 phase. The effect of Tip60-p400 HAT component knockdown was
unique to ES cells, as negligible changes were observed following
knockdown in mouse embryonic fibroblasts.
Telomerase is a ribonucleoprotein (RNP) complex consisting of a protein
subunit, TERT (187270), an RNA subunit, TERC (602322), and the
TERC-binding protein dyskerin (DKC1; 300126). Using affinity
chromatography and mass spectrometry, Venteicher et al. (2008)
identified pontin (RUVBL1) and reptin as components of the telomerase
complex in HeLa cells. Pontin interacted directly with both TERT and
dyskerin. The amount of TERT bound to pontin and reptin peaked in S
phase. Depletion of pontin and reptin impaired telomerase RNP
accumulation, indicating an essential role for these proteins in
telomerase assembly.
GENE STRUCTURE
Parfait et al. (2000) reported the gene structure of TIP49B/RUVBL2.
RUVBL2 contains 15 exons.
MAPPING
Parfait et al. (2000) showed that the RUVBL2 gene is physically linked
to the CGB (118860)/LHB (152780) gene cluster on 19q13.3. Genomic
sequence analysis revealed that the RUVBL2 gene is very close (55
nucleotides in length) to the LHB gene, in the opposite orientation of
transcription. The very close colocalization of the mouse homologs of
the human RUVBL2 and LHB genes is also conserved on mouse chromosome 7.
Coordinated transcriptional regulation of the RUVBL2 and LHB genes was
not observed.
*FIELD* RF
1. Doyon, Y.; Selleck, W.; Lane, W. S.; Tan, S.; Cote, J.: Structural
and functional conservation of the NuA4 histone acetyltransferase
complex from yeast to humans. Molec. Cell. Biol. 24: 1884-1896,
2004.
2. Fazzio, T. G.; Huff, J. T.; Panning, B.: An RNAi screen of chromatin
proteins identifies Tip60-p400 as a regulator of embryonic stem cell
identity. Cell 134: 162-174, 2008.
3. Kanemaki, M.; Kurokawa, Y.; Matsu-ura, T.; Makino, Y.; Masani,
A.; Okazaki, K.; Morishita, T.; Tamura, T.: TIP49b, a new RuvB-like
DNA helicase, is included in a complex together with another RuvB-like
DNA helicase, TIP49a. J. Biol. Chem. 274: 22437-22444, 1999.
4. Parfait, B.; Giovangrandi, Y.; Asheuer, M.; Laurendeau, I.; Olivi,
M.; Vodovar, N.; Vidaud, D.; Vidaud, M.; Bieche, I.: Human TIP49b/RUVBL2
gene: genomic structure, expression pattern, physical link to the
human CGB/LHB gene cluster on chromosome 19q13.3. Ann. de Genet. 43:
69-74, 2000.
5. Salzer, U.; Kubicek, M.; Prohaska, R.: Isolation, molecular characterization,
and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous,
interacting erythroid cytosolic proteins. Biochim. Biophys. Acta 1446:
365-370, 1999.
6. Venteicher, A. S.; Meng, Z.; Mason, P. J.; Veenstra, T. D.; Artandi,
S. E.: Identification of ATPases pontin and reptin as telomerase
components essential for holoenzyme assembly. Cell 132: 945-957,
2008.
7. Wood, M. A.; McMahon, S. B.; Cole, M. D.: An ATPase/helicase complex
is an essential cofactor for oncogenic transformation by c-Myc. Molec.
Cell 5: 321-330, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2008
Patricia A. Hartz - updated: 5/29/2008
Matthew B. Gross - updated: 5/8/2007
Paul J. Converse - updated: 2/16/2001
Victor A. McKusick - updated: 2/13/2001
*FIELD* CD
Stylianos E. Antonarakis: 4/4/2000
*FIELD* ED
mgross: 02/08/2013
mgross: 1/11/2013
mgross: 11/7/2008
terry: 11/5/2008
mgross: 5/30/2008
terry: 5/29/2008
mgross: 5/8/2007
alopez: 9/20/2005
mgross: 2/28/2001
terry: 2/16/2001
carol: 2/15/2001
cwells: 2/15/2001
cwells: 2/14/2001
terry: 2/13/2001
mgross: 4/4/2000
*RECORD*
*FIELD* NO
604788
*FIELD* TI
*604788 RUVB, E. COLI, HOMOLOG-LIKE 2; RUVBL2
;;TATA BOX-BINDING PROTEIN-INTERACTING PROTEIN, 48-KD; TIP48;;
read moreTBP-INTERACTING PROTEIN, 48-KD;;
TIP49B;;
REPTIN;;
ERYTHROCYTE CYTOSOLIC PROTEIN, 51-KD; ECP51
*FIELD* TX
CLONING
Most organisms contain multiple DNA helicases that catalyze the
unwinding of double-stranded DNA to single-stranded DNA in an
ATP-dependent manner, an essential process in replication, repair, and
transcription. RuvB is a bacterial DNA helicase involved in homologous
recombination and double-strand break repair. By amplifying sequences
related to 2 EST clones, Kanemaki et al. (1999) obtained a cDNA encoding
RuvB-like-2 (RUVBL2), which they termed TIP49B. The deduced 463-amino
acid protein contains Walker A and B motifs and is highly similar
structurally to other TIP49 family proteins, including TIP49A (RUVBL1;
603449). Western blot analysis revealed that, similar to RUVBL1, RUVBL2
is ubiquitously expressed, with highest levels in testis and thymus.
Using affinity chromatography of erythrocyte cytosol, followed by
micropeptide sequence analysis, EST database searching, PCR, and RACE,
Salzer et al. (1999) isolated cDNAs encoding RUVBL1 and RUVBL2, which
they termed ECP54 and ECP51, respectively. Northern blot analysis
revealed wide expression of a 1.5-kb RUVBL2 transcript that was most
abundant in heart, skeletal muscle, and testis.
Wood et al. (2000) identified human homologs of the RuvB protein. By use
of the MYC (190080) transactivation domain to affinity purify tightly
associated nuclear proteins, they identified RUVBL1 and RUVBL2, which
they called TIP48. RUVBL1 and RUVBL2 are both highly conserved in
evolution and contain ATPase/helicase motifs. The RUVBL2 protein
contains 463 amino acids and shares 45% amino acid identity with RUVBL1.
By RT-PCR, Parfait et al. (2000) found that RUVBL2, like RUVBL1, is
ubiquitously expressed in human tissues, with highest expression in
testis.
GENE FUNCTION
Functional analysis by Kanemaki et al. (1999) showed that RUVBL2 has
both ATPase and DNA helicase (preferentially moving in the 5-prime to
3-prime direction) activity and that RUVBL2 binds to RUVBL1.
Coimmunoprecipitation assays determined that RUVBL1 and RUVBL2 are
included in an approximately 700-kD complex in the cell nucleus. Gene
disruption analysis showed that like RUVBL1, RUVBL2 is an essential gene
for growth in yeast.
Wood et al. (2000) found that RUVBL1 and RUVBL2 are complexed with MYC
in vivo, and binding is dependent on a MYC domain essential for
oncogenic activity.
The NuA4 histone acetyltransferase (HAT) complex is responsible for
acetylation of the N-terminal tails of histone H4 (see 602822) and H2A
(see 613499) in yeast. Its catalytic subunit, Esa1, is homologous to
human TIP60 (HTATIP; 601409). Using affinity purification, Western blot
analysis, cell fractionation, immunoprecipitation, and mass
spectrometry, Doyon et al. (2004) found that TIP60 and its splice
variant, TIP60B/PLIP, were part of a multisubunit NuA4 complex with HAT
activity in several human cell lines. They identified RUVBL2 as 1 of 3
subunits specific to the human NuA4 HAT complex.
Using RNA interference in mouse embryonic stem (ES) cells, Fazzio et al.
(2008) found that depletion of any of 7 components of the Tip60-p400
(EP400; 606265) HAT and nucleosome remodeling complex, including Ruvbl2,
caused the same phenotype. Unlike normal ES cells, which grow in
spherical 3-dimensional colonies, ES cells depleted of any the 7
Tip60-p400 HAT components showed a flattened and elongated morphology,
with monolayer growth and reduced cell-cell contacts. These knockdown
cells continued to cycle, with reduced cells in S phase and increased
cells in G2 phase. The effect of Tip60-p400 HAT component knockdown was
unique to ES cells, as negligible changes were observed following
knockdown in mouse embryonic fibroblasts.
Telomerase is a ribonucleoprotein (RNP) complex consisting of a protein
subunit, TERT (187270), an RNA subunit, TERC (602322), and the
TERC-binding protein dyskerin (DKC1; 300126). Using affinity
chromatography and mass spectrometry, Venteicher et al. (2008)
identified pontin (RUVBL1) and reptin as components of the telomerase
complex in HeLa cells. Pontin interacted directly with both TERT and
dyskerin. The amount of TERT bound to pontin and reptin peaked in S
phase. Depletion of pontin and reptin impaired telomerase RNP
accumulation, indicating an essential role for these proteins in
telomerase assembly.
GENE STRUCTURE
Parfait et al. (2000) reported the gene structure of TIP49B/RUVBL2.
RUVBL2 contains 15 exons.
MAPPING
Parfait et al. (2000) showed that the RUVBL2 gene is physically linked
to the CGB (118860)/LHB (152780) gene cluster on 19q13.3. Genomic
sequence analysis revealed that the RUVBL2 gene is very close (55
nucleotides in length) to the LHB gene, in the opposite orientation of
transcription. The very close colocalization of the mouse homologs of
the human RUVBL2 and LHB genes is also conserved on mouse chromosome 7.
Coordinated transcriptional regulation of the RUVBL2 and LHB genes was
not observed.
*FIELD* RF
1. Doyon, Y.; Selleck, W.; Lane, W. S.; Tan, S.; Cote, J.: Structural
and functional conservation of the NuA4 histone acetyltransferase
complex from yeast to humans. Molec. Cell. Biol. 24: 1884-1896,
2004.
2. Fazzio, T. G.; Huff, J. T.; Panning, B.: An RNAi screen of chromatin
proteins identifies Tip60-p400 as a regulator of embryonic stem cell
identity. Cell 134: 162-174, 2008.
3. Kanemaki, M.; Kurokawa, Y.; Matsu-ura, T.; Makino, Y.; Masani,
A.; Okazaki, K.; Morishita, T.; Tamura, T.: TIP49b, a new RuvB-like
DNA helicase, is included in a complex together with another RuvB-like
DNA helicase, TIP49a. J. Biol. Chem. 274: 22437-22444, 1999.
4. Parfait, B.; Giovangrandi, Y.; Asheuer, M.; Laurendeau, I.; Olivi,
M.; Vodovar, N.; Vidaud, D.; Vidaud, M.; Bieche, I.: Human TIP49b/RUVBL2
gene: genomic structure, expression pattern, physical link to the
human CGB/LHB gene cluster on chromosome 19q13.3. Ann. de Genet. 43:
69-74, 2000.
5. Salzer, U.; Kubicek, M.; Prohaska, R.: Isolation, molecular characterization,
and tissue-specific expression of ECP-51 and ECP-54 (TIP49), two homologous,
interacting erythroid cytosolic proteins. Biochim. Biophys. Acta 1446:
365-370, 1999.
6. Venteicher, A. S.; Meng, Z.; Mason, P. J.; Veenstra, T. D.; Artandi,
S. E.: Identification of ATPases pontin and reptin as telomerase
components essential for holoenzyme assembly. Cell 132: 945-957,
2008.
7. Wood, M. A.; McMahon, S. B.; Cole, M. D.: An ATPase/helicase complex
is an essential cofactor for oncogenic transformation by c-Myc. Molec.
Cell 5: 321-330, 2000.
*FIELD* CN
Patricia A. Hartz - updated: 11/5/2008
Patricia A. Hartz - updated: 5/29/2008
Matthew B. Gross - updated: 5/8/2007
Paul J. Converse - updated: 2/16/2001
Victor A. McKusick - updated: 2/13/2001
*FIELD* CD
Stylianos E. Antonarakis: 4/4/2000
*FIELD* ED
mgross: 02/08/2013
mgross: 1/11/2013
mgross: 11/7/2008
terry: 11/5/2008
mgross: 5/30/2008
terry: 5/29/2008
mgross: 5/8/2007
alopez: 9/20/2005
mgross: 2/28/2001
terry: 2/16/2001
carol: 2/15/2001
cwells: 2/15/2001
cwells: 2/14/2001
terry: 2/13/2001
mgross: 4/4/2000