Full text data of RUVBL1
RUVBL1
(INO80H, NMP238, TIP49, TIP49A)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
RuvB-like 1; 3.6.4.12 (49 kDa TATA box-binding protein-interacting protein; 49 kDa TBP-interacting protein; 54 kDa erythrocyte cytosolic protein; ECP-54; INO80 complex subunit H; Nuclear matrix protein 238; NMP 238; Pontin 52; TIP49a; TIP60-associated protein 54-alpha; TAP54-alpha)
RuvB-like 1; 3.6.4.12 (49 kDa TATA box-binding protein-interacting protein; 49 kDa TBP-interacting protein; 54 kDa erythrocyte cytosolic protein; ECP-54; INO80 complex subunit H; Nuclear matrix protein 238; NMP 238; Pontin 52; TIP49a; TIP60-associated protein 54-alpha; TAP54-alpha)
UniProt
Q9Y265
ID RUVB1_HUMAN Reviewed; 456 AA.
AC Q9Y265; B2R5S0; P82276; Q1KMR0; Q53HK5; Q53HL7; Q53Y27; Q9BSX9;
read moreDT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=RuvB-like 1;
DE EC=3.6.4.12;
DE AltName: Full=49 kDa TATA box-binding protein-interacting protein;
DE Short=49 kDa TBP-interacting protein;
DE AltName: Full=54 kDa erythrocyte cytosolic protein;
DE Short=ECP-54;
DE AltName: Full=INO80 complex subunit H;
DE AltName: Full=Nuclear matrix protein 238;
DE Short=NMP 238;
DE AltName: Full=Pontin 52;
DE AltName: Full=TIP49a;
DE AltName: Full=TIP60-associated protein 54-alpha;
DE Short=TAP54-alpha;
GN Name=RUVBL1; Synonyms=INO80H, NMP238, TIP49, TIP49A;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9588198; DOI=10.1006/bbrc.1998.8504;
RA Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S.,
RA Kishimoto T., Tamura T.-A.;
RT "TIP49, homologous to the bacterial DNA helicase RuvB, acts as an
RT autoantigen in human.";
RL Biochem. Biophys. Res. Commun. 245:819-823(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 1-7.
RC TISSUE=Pancreas;
RX PubMed=9813143; DOI=10.1006/bbrc.1998.9604;
RA Holzmann K., Gerner C., Korosec T., Poeltl A., Grimm R., Sauermann G.;
RT "Identification and characterization of the ubiquitously occurring
RT nuclear matrix protein NMP 238.";
RL Biochem. Biophys. Res. Commun. 252:39-45(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9774387; DOI=10.1074/jbc.273.43.27786;
RA Qiu X.-B., Lin Y.-L., Thome K.C., Pian P., Schlegel B.P.,
RA Weremowicz S., Parvin J.D., Dutta A.;
RT "An eukaryotic RuvB-like protein (RUVBL1) essential for growth.";
RL J. Biol. Chem. 273:27786-27793(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9843967; DOI=10.1073/pnas.95.25.14787;
RA Bauer A., Huber O., Kemler R.;
RT "Pontin52, an interaction partner of beta-catenin, binds to the TATA
RT box binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 34-46;
RP 108-118; 169-177; 207-219 AND 446-456.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182
RP AND 184-201, AND FUNCTION.
RX PubMed=11027681; DOI=10.1074/jbc.M004919200;
RA Hawley S.B., Tamura T.-A., Miles L.A.;
RT "Purification, cloning, and characterization of a profibrinolytic
RT plasminogen-binding protein, TIP49a.";
RL J. Biol. Chem. 276:179-186(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Huber O., Orso S.;
RT "The genomic structure of the human pontin 52 gene.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Koc F., Gartner W., Birkenkamp-Demtroeder K., Altenberger T.,
RA Daneva T., Wagner L.;
RT "RUVBL1-FK- splice variant.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue, and Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [14]
RP PROTEIN SEQUENCE OF 23-33; 65-90; 153-162; 172-182; 318-333; 340-357;
RP 363-372 AND 379-400, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 23-33 AND 77-90, INTERACTION WITH MYC, AND
RP MUTAGENESIS OF ASP-302.
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 [16]
RP PROTEIN SEQUENCE OF 23-33; 34-46; 77-90; 172-182; 185-201; 340-357 AND
RP 405-418 (ISOFORM 1), 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 [17]
RP PROTEIN SEQUENCE OF 34-46 AND 108-117, IDENTIFICATION IN NUA4 COMPLEX,
RP 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 [18]
RP PROTEIN SEQUENCE OF 34-46, FUNCTION, INTERACTION WITH TUBULIN, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Monocyte;
RX PubMed=14506706; DOI=10.1002/cm.10136;
RA Gartner W., Rossbacher J., Zierhut B., Daneva T., Base W., Weissel M.,
RA Waldhausl W., Pasternack M.S., Wagner L.;
RT "The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin
RT during mitosis.";
RL Cell Motil. Cytoskeleton 56:79-93(2003).
RN [19]
RP INTERACTION WITH RUVBL2.
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 [20]
RP FUNCTION.
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 [21]
RP IDENTIFICATION IN BAF53 COMPLEX WITH ACTL6A; SMARCA2 AND TRRAP.
RX PubMed=11839798; DOI=10.1128/MCB.22.5.1307-1316.2002;
RA Park J., Wood M.A., Cole M.D.;
RT "BAF53 forms distinct nuclear complexes and functions as a critical c-
RT Myc-interacting nuclear cofactor for oncogenic transformation.";
RL Mol. Cell. Biol. 22:1307-1316(2002).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF ASP-302.
RX PubMed=14695187;
RA Feng Y., Lee N., Fearon E.R.;
RT "TIP49 regulates beta-catenin-mediated neoplastic transformation and
RT T-cell factor target gene induction via effects on chromatin
RT remodeling.";
RL Cancer Res. 63:8726-8734(2003).
RN [23]
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 [24]
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 [25]
RP IDENTIFICATION IN THE 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 [26]
RP INTERACTION WITH HINT1, FUNCTION, AND SUBCELLULAR LOCATION.
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 [27]
RP SUBUNIT, MUTAGENESIS OF ASP-302, 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 [28]
RP INTERACTION WITH OFD1.
RX PubMed=17761535; DOI=10.1091/mbc.E07-03-0198;
RA Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S.,
RA Franco B.;
RT "Functional characterization of the OFD1 protein reveals a nuclear
RT localization and physical interaction with subunits of a chromatin
RT remodeling complex.";
RL Mol. Biol. Cell 18:4397-4404(2007).
RN [29]
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 [30]
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 [31]
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [33]
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 [34]
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 [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [36]
RP IDENTIFICATION IN A COMPLEX WITH USP49 AND PSMC5.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP ASP-302.
RX PubMed=17060327; DOI=10.1074/jbc.M605625200;
RA Matias P.M., Gorynia S., Donner P., Carrondo M.A.;
RT "Crystal structure of the human AAA+ protein RuvBL1.";
RL J. Biol. Chem. 281:38918-38929(2006).
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (3' to 5') 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. Essential for cell proliferation.
CC -!- FUNCTION: May be able to bind plasminogen at cell surface and
CC enhance plasminogen activation.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Forms homohexameric rings. Can form a dodecamer with
CC RUVBL2 made of two stacked hexameric rings; however, even though
CC RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric
CC status of each hexamer is not known. Oligomerization may regulate
CC binding to nucleic acids and conversely, binding to nucleic acids
CC may affect the dodecameric assembly. Interacts with the
CC transcriptional activation domain of MYC. Component of the RNA
CC polymerase II holoenzyme complex. May also act to bridge the
CC LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone
CC acetyltransferase complex which contains the catalytic subunit
CC KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A,
CC MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and
CC MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A
CC protein. RUVBL1 interacts with EP400. Component of a NuA4-related
CC complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP,
CC EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A,
CC VPS72 and YEATS4/GAS41. Component of the BAF53 complex, at least
CC composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and
CC TRRAP/PAF400. Component of some MLL1/MLL complex, at least
CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1,
CC WDR5 and RBBP5, as well as the facultative components BAP18, CHD8,
CC E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF,
CC PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3,
CC TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Associates with alpha and
CC gamma tubulins, particularly during metaphase and early anaphase.
CC Interacts with NPAT. Component of the chromatin-remodeling INO80
CC complex; specifically part of a complex module associated with the
CC helicase ATP-binding and the helicase C-terminal domain of INO80.
CC Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1.
CC Component of a complex with USP49 and PSMC5.
CC -!- INTERACTION:
CC O60832:DKC1; NbExp=8; IntAct=EBI-353675, EBI-713091;
CC Q9Y230:RUVBL2; NbExp=21; IntAct=EBI-353675, EBI-352939;
CC O14746:TERT; NbExp=11; IntAct=EBI-353675, EBI-1772203;
CC Q15906:VPS72; NbExp=6; IntAct=EBI-353675, EBI-399189;
CC P25490:YY1; NbExp=4; IntAct=EBI-353675, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
CC Cytoplasm. Membrane. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Mainly localized in the
CC nucleus, associated with nuclear matrix or in the nuclear cytosol,
CC although it is also present in the cytoplasm and associated with
CC the cell membranes. In prophase and prometaphase it is located at
CC the centrosome and the branching microtubule spindles. After
CC mitotic nuclear membrane disintigration it accumulates at the
CC centrosome and sites of tubulin polymerization. As cells pass
CC through metaphase and into telophase it is located close to the
CC centrosome at the early phase of tubulin polymerization. In
CC anaphase it accumulates at the zone of tubule interdigitation. In
CC telophase it is found at polar tubule overlap, and it reappears at
CC the site of chromosomal decondensation in the daughter cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y265-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y265-2; Sequence=VSP_021387, VSP_021388;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
CC heart, skeletal muscle and testis.
CC -!- DOMAIN: Binding to MYC is dependent on a Myc domain essential for
CC oncogenic activity.
CC -!- MISCELLANEOUS: High level of autoantibodies against RUVBL1 are
CC detected in sera of patients with autoimmune diseases such as
CC polymyositis/dermatomyosistis and autoimmune hepatitis.
CC -!- SIMILARITY: Belongs to the RuvB family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL1ID44415ch3q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB012122; BAA28169.1; -; mRNA.
DR EMBL; AJ010058; CAA08986.1; -; mRNA.
DR EMBL; AF070735; AAC77819.1; -; mRNA.
DR EMBL; AF099084; AAD04427.1; -; mRNA.
DR EMBL; Y18418; CAB46271.1; -; mRNA.
DR EMBL; AF380344; AAM45570.1; -; Genomic_DNA.
DR EMBL; AF380343; AAM45570.1; JOINED; Genomic_DNA.
DR EMBL; DQ469310; ABF13334.1; -; mRNA.
DR EMBL; BT007057; AAP35706.1; -; mRNA.
DR EMBL; AK222563; BAD96283.1; -; mRNA.
DR EMBL; AK222575; BAD96295.1; -; mRNA.
DR EMBL; AK312290; BAG35217.1; -; mRNA.
DR EMBL; AB451224; BAG70038.1; -; mRNA.
DR EMBL; BC002993; AAH02993.1; -; mRNA.
DR EMBL; BC012886; AAH12886.1; -; mRNA.
DR PIR; JE0334; JE0334.
DR RefSeq; NP_003698.1; NM_003707.2.
DR RefSeq; XP_005247899.1; XM_005247842.1.
DR UniGene; Hs.272822; -.
DR PDB; 2C9O; X-ray; 2.20 A; A/B/C=1-456.
DR PDB; 2XSZ; X-ray; 3.00 A; A/B/C=2-456.
DR PDBsum; 2C9O; -.
DR PDBsum; 2XSZ; -.
DR ProteinModelPortal; Q9Y265; -.
DR SMR; Q9Y265; 7-453.
DR DIP; DIP-29937N; -.
DR IntAct; Q9Y265; 71.
DR MINT; MINT-1138777; -.
DR STRING; 9606.ENSP00000318297; -.
DR PhosphoSite; Q9Y265; -.
DR DMDM; 28201891; -.
DR OGP; Q9Y265; -.
DR REPRODUCTION-2DPAGE; Q9Y265; -.
DR SWISS-2DPAGE; Q9Y265; -.
DR PaxDb; Q9Y265; -.
DR PeptideAtlas; Q9Y265; -.
DR PRIDE; Q9Y265; -.
DR DNASU; 8607; -.
DR Ensembl; ENST00000322623; ENSP00000318297; ENSG00000175792.
DR Ensembl; ENST00000417360; ENSP00000393755; ENSG00000175792.
DR GeneID; 8607; -.
DR KEGG; hsa:8607; -.
DR UCSC; uc003ekh.3; human.
DR CTD; 8607; -.
DR GeneCards; GC03M127783; -.
DR HGNC; HGNC:10474; RUVBL1.
DR HPA; HPA019947; -.
DR HPA; HPA019948; -.
DR MIM; 603449; gene.
DR neXtProt; NX_Q9Y265; -.
DR PharmGKB; PA34887; -.
DR eggNOG; COG1224; -.
DR HOVERGEN; HBG054186; -.
DR InParanoid; Q9Y265; -.
DR KO; K04499; -.
DR OMA; NKVVSKY; -.
DR PhylomeDB; Q9Y265; -.
DR Reactome; REACT_115566; Cell Cycle.
DR ChiTaRS; RUVBL1; human.
DR EvolutionaryTrace; Q9Y265; -.
DR GeneWiki; RuvB-like_1; -.
DR GenomeRNAi; 8607; -.
DR NextBio; 32249; -.
DR PRO; PR:Q9Y265; -.
DR ArrayExpress; Q9Y265; -.
DR Bgee; Q9Y265; -.
DR CleanEx; HS_RUVBL1; -.
DR Genevestigator; Q9Y265; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW ATP-binding; Cell cycle; Cell division; Chromatin regulator;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; Growth regulation;
KW Helicase; Hydrolase; Membrane; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 456 RuvB-like 1.
FT /FTId=PRO_0000165639.
FT NP_BIND 70 77 ATP (By similarity).
FT MOD_RES 453 453 N6-acetyllysine.
FT VAR_SEQ 374 386 IIKIRAQTEGINI -> VLSAAADPGQLAC (in
FT isoform 2).
FT /FTId=VSP_021387.
FT VAR_SEQ 387 456 Missing (in isoform 2).
FT /FTId=VSP_021388.
FT MUTAGEN 302 302 D->N: Abolishes ATPase activity;
FT inhibition of MYC- and CTNNB1-mediated
FT transformation.
FT CONFLICT 52 52 I -> T (in Ref. 12; BAD96283).
FT CONFLICT 145 145 N -> D (in Ref. 12; BAD96295).
FT CONFLICT 285 285 K -> R (in Ref. 8; ABF13334).
FT CONFLICT 353 353 D -> P (in Ref. 8; ABF13334).
FT HELIX 10 16
FT TURN 17 20
FT STRAND 28 30
FT STRAND 34 36
FT STRAND 39 41
FT HELIX 43 57
FT STRAND 65 69
FT STRAND 72 75
FT HELIX 76 87
FT STRAND 93 97
FT HELIX 98 101
FT STRAND 104 106
FT HELIX 108 118
FT STRAND 119 140
FT STRAND 157 163
FT STRAND 166 172
FT HELIX 174 182
FT STRAND 189 194
FT TURN 195 197
FT STRAND 200 206
FT STRAND 216 221
FT STRAND 228 239
FT HELIX 240 245
FT HELIX 278 288
FT STRAND 291 296
FT STRAND 298 303
FT HELIX 304 306
FT HELIX 309 318
FT STRAND 326 331
FT STRAND 334 337
FT STRAND 345 347
FT HELIX 352 355
FT STRAND 358 362
FT HELIX 368 382
FT HELIX 388 400
FT HELIX 403 408
FT HELIX 410 419
FT STRAND 423 425
FT HELIX 427 436
FT HELIX 440 448
SQ SEQUENCE 456 AA; 50228 MW; 6095ADE692B1482B CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK
//
ID RUVB1_HUMAN Reviewed; 456 AA.
AC Q9Y265; B2R5S0; P82276; Q1KMR0; Q53HK5; Q53HL7; Q53Y27; Q9BSX9;
read moreDT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=RuvB-like 1;
DE EC=3.6.4.12;
DE AltName: Full=49 kDa TATA box-binding protein-interacting protein;
DE Short=49 kDa TBP-interacting protein;
DE AltName: Full=54 kDa erythrocyte cytosolic protein;
DE Short=ECP-54;
DE AltName: Full=INO80 complex subunit H;
DE AltName: Full=Nuclear matrix protein 238;
DE Short=NMP 238;
DE AltName: Full=Pontin 52;
DE AltName: Full=TIP49a;
DE AltName: Full=TIP60-associated protein 54-alpha;
DE Short=TAP54-alpha;
GN Name=RUVBL1; Synonyms=INO80H, NMP238, TIP49, TIP49A;
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] (ISOFORM 1).
RC TISSUE=Liver;
RX PubMed=9588198; DOI=10.1006/bbrc.1998.8504;
RA Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S.,
RA Kishimoto T., Tamura T.-A.;
RT "TIP49, homologous to the bacterial DNA helicase RuvB, acts as an
RT autoantigen in human.";
RL Biochem. Biophys. Res. Commun. 245:819-823(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 1-7.
RC TISSUE=Pancreas;
RX PubMed=9813143; DOI=10.1006/bbrc.1998.9604;
RA Holzmann K., Gerner C., Korosec T., Poeltl A., Grimm R., Sauermann G.;
RT "Identification and characterization of the ubiquitously occurring
RT nuclear matrix protein NMP 238.";
RL Biochem. Biophys. Res. Commun. 252:39-45(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=9774387; DOI=10.1074/jbc.273.43.27786;
RA Qiu X.-B., Lin Y.-L., Thome K.C., Pian P., Schlegel B.P.,
RA Weremowicz S., Parvin J.D., Dutta A.;
RT "An eukaryotic RuvB-like protein (RUVBL1) essential for growth.";
RL J. Biol. Chem. 273:27786-27793(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Colon adenocarcinoma;
RX PubMed=9843967; DOI=10.1073/pnas.95.25.14787;
RA Bauer A., Huber O., Kemler R.;
RT "Pontin52, an interaction partner of beta-catenin, binds to the TATA
RT box binding protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 34-46;
RP 108-118; 169-177; 207-219 AND 446-456.
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182
RP AND 184-201, AND FUNCTION.
RX PubMed=11027681; DOI=10.1074/jbc.M004919200;
RA Hawley S.B., Tamura T.-A., Miles L.A.;
RT "Purification, cloning, and characterization of a profibrinolytic
RT plasminogen-binding protein, TIP49a.";
RL J. Biol. Chem. 276:179-186(2001).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
RA Huber O., Orso S.;
RT "The genomic structure of the human pontin 52 gene.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Koc F., Gartner W., Birkenkamp-Demtroeder K., Altenberger T.,
RA Daneva T., Wagner L.;
RT "RUVBL1-FK- splice variant.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Cerebellum;
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 [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adipose tissue, and Coronary artery;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [13]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [14]
RP PROTEIN SEQUENCE OF 23-33; 65-90; 153-162; 172-182; 318-333; 340-357;
RP 363-372 AND 379-400, AND MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 23-33 AND 77-90, INTERACTION WITH MYC, AND
RP MUTAGENESIS OF ASP-302.
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 [16]
RP PROTEIN SEQUENCE OF 23-33; 34-46; 77-90; 172-182; 185-201; 340-357 AND
RP 405-418 (ISOFORM 1), 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 [17]
RP PROTEIN SEQUENCE OF 34-46 AND 108-117, IDENTIFICATION IN NUA4 COMPLEX,
RP 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 [18]
RP PROTEIN SEQUENCE OF 34-46, FUNCTION, INTERACTION WITH TUBULIN, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Monocyte;
RX PubMed=14506706; DOI=10.1002/cm.10136;
RA Gartner W., Rossbacher J., Zierhut B., Daneva T., Base W., Weissel M.,
RA Waldhausl W., Pasternack M.S., Wagner L.;
RT "The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin
RT during mitosis.";
RL Cell Motil. Cytoskeleton 56:79-93(2003).
RN [19]
RP INTERACTION WITH RUVBL2.
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 [20]
RP FUNCTION.
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 [21]
RP IDENTIFICATION IN BAF53 COMPLEX WITH ACTL6A; SMARCA2 AND TRRAP.
RX PubMed=11839798; DOI=10.1128/MCB.22.5.1307-1316.2002;
RA Park J., Wood M.A., Cole M.D.;
RT "BAF53 forms distinct nuclear complexes and functions as a critical c-
RT Myc-interacting nuclear cofactor for oncogenic transformation.";
RL Mol. Cell. Biol. 22:1307-1316(2002).
RN [22]
RP FUNCTION, AND MUTAGENESIS OF ASP-302.
RX PubMed=14695187;
RA Feng Y., Lee N., Fearon E.R.;
RT "TIP49 regulates beta-catenin-mediated neoplastic transformation and
RT T-cell factor target gene induction via effects on chromatin
RT remodeling.";
RL Cancer Res. 63:8726-8734(2003).
RN [23]
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 [24]
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 [25]
RP IDENTIFICATION IN THE 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 [26]
RP INTERACTION WITH HINT1, FUNCTION, AND SUBCELLULAR LOCATION.
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 [27]
RP SUBUNIT, MUTAGENESIS OF ASP-302, 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 [28]
RP INTERACTION WITH OFD1.
RX PubMed=17761535; DOI=10.1091/mbc.E07-03-0198;
RA Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S.,
RA Franco B.;
RT "Functional characterization of the OFD1 protein reveals a nuclear
RT localization and physical interaction with subunits of a chromatin
RT remodeling complex.";
RL Mol. Biol. Cell 18:4397-4404(2007).
RN [29]
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 [30]
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 [31]
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [33]
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 [34]
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 [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [36]
RP IDENTIFICATION IN A COMPLEX WITH USP49 AND PSMC5.
RX PubMed=23824326; DOI=10.1101/gad.211037.112;
RA Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
RA Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
RA Giles K.E., Ma L., Wang H.;
RT "USP49 deubiquitinates histone H2B and regulates cotranscriptional
RT pre-mRNA splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [37]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
RP ASP-302.
RX PubMed=17060327; DOI=10.1074/jbc.M605625200;
RA Matias P.M., Gorynia S., Donner P., Carrondo M.A.;
RT "Crystal structure of the human AAA+ protein RuvBL1.";
RL J. Biol. Chem. 281:38918-38929(2006).
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (3' to 5') 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. Essential for cell proliferation.
CC -!- FUNCTION: May be able to bind plasminogen at cell surface and
CC enhance plasminogen activation.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
CC -!- SUBUNIT: Forms homohexameric rings. Can form a dodecamer with
CC RUVBL2 made of two stacked hexameric rings; however, even though
CC RUVBL1 and RUVBL2 are present in equimolar ratio, the oligomeric
CC status of each hexamer is not known. Oligomerization may regulate
CC binding to nucleic acids and conversely, binding to nucleic acids
CC may affect the dodecameric assembly. Interacts with the
CC transcriptional activation domain of MYC. Component of the RNA
CC polymerase II holoenzyme complex. May also act to bridge the
CC LEF1/TCF1-CTNNB1 complex and TBP. Component of the NuA4 histone
CC acetyltransferase complex which contains the catalytic subunit
CC KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A,
CC MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and
CC MEAF6. The NuA4 complex interacts with MYC and the adenovirus E1A
CC protein. RUVBL1 interacts with EP400. Component of a NuA4-related
CC complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP,
CC EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A,
CC VPS72 and YEATS4/GAS41. Component of the BAF53 complex, at least
CC composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and
CC TRRAP/PAF400. Component of some MLL1/MLL complex, at least
CC composed of the core components KMT2A/MLL1, ASH2L, HCFC1/HCF1,
CC WDR5 and RBBP5, as well as the facultative components BAP18, CHD8,
CC E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA, MYST1/MOF,
CC PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B, SENP3,
CC TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Associates with alpha and
CC gamma tubulins, particularly during metaphase and early anaphase.
CC Interacts with NPAT. Component of the chromatin-remodeling INO80
CC complex; specifically part of a complex module associated with the
CC helicase ATP-binding and the helicase C-terminal domain of INO80.
CC Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1.
CC Component of a complex with USP49 and PSMC5.
CC -!- INTERACTION:
CC O60832:DKC1; NbExp=8; IntAct=EBI-353675, EBI-713091;
CC Q9Y230:RUVBL2; NbExp=21; IntAct=EBI-353675, EBI-352939;
CC O14746:TERT; NbExp=11; IntAct=EBI-353675, EBI-1772203;
CC Q15906:VPS72; NbExp=6; IntAct=EBI-353675, EBI-399189;
CC P25490:YY1; NbExp=4; IntAct=EBI-353675, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
CC Cytoplasm. Membrane. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Mainly localized in the
CC nucleus, associated with nuclear matrix or in the nuclear cytosol,
CC although it is also present in the cytoplasm and associated with
CC the cell membranes. In prophase and prometaphase it is located at
CC the centrosome and the branching microtubule spindles. After
CC mitotic nuclear membrane disintigration it accumulates at the
CC centrosome and sites of tubulin polymerization. As cells pass
CC through metaphase and into telophase it is located close to the
CC centrosome at the early phase of tubulin polymerization. In
CC anaphase it accumulates at the zone of tubule interdigitation. In
CC telophase it is found at polar tubule overlap, and it reappears at
CC the site of chromosomal decondensation in the daughter cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y265-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y265-2; Sequence=VSP_021387, VSP_021388;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
CC heart, skeletal muscle and testis.
CC -!- DOMAIN: Binding to MYC is dependent on a Myc domain essential for
CC oncogenic activity.
CC -!- MISCELLANEOUS: High level of autoantibodies against RUVBL1 are
CC detected in sera of patients with autoimmune diseases such as
CC polymyositis/dermatomyosistis and autoimmune hepatitis.
CC -!- SIMILARITY: Belongs to the RuvB family.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC and Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL1ID44415ch3q21.html";
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AB012122; BAA28169.1; -; mRNA.
DR EMBL; AJ010058; CAA08986.1; -; mRNA.
DR EMBL; AF070735; AAC77819.1; -; mRNA.
DR EMBL; AF099084; AAD04427.1; -; mRNA.
DR EMBL; Y18418; CAB46271.1; -; mRNA.
DR EMBL; AF380344; AAM45570.1; -; Genomic_DNA.
DR EMBL; AF380343; AAM45570.1; JOINED; Genomic_DNA.
DR EMBL; DQ469310; ABF13334.1; -; mRNA.
DR EMBL; BT007057; AAP35706.1; -; mRNA.
DR EMBL; AK222563; BAD96283.1; -; mRNA.
DR EMBL; AK222575; BAD96295.1; -; mRNA.
DR EMBL; AK312290; BAG35217.1; -; mRNA.
DR EMBL; AB451224; BAG70038.1; -; mRNA.
DR EMBL; BC002993; AAH02993.1; -; mRNA.
DR EMBL; BC012886; AAH12886.1; -; mRNA.
DR PIR; JE0334; JE0334.
DR RefSeq; NP_003698.1; NM_003707.2.
DR RefSeq; XP_005247899.1; XM_005247842.1.
DR UniGene; Hs.272822; -.
DR PDB; 2C9O; X-ray; 2.20 A; A/B/C=1-456.
DR PDB; 2XSZ; X-ray; 3.00 A; A/B/C=2-456.
DR PDBsum; 2C9O; -.
DR PDBsum; 2XSZ; -.
DR ProteinModelPortal; Q9Y265; -.
DR SMR; Q9Y265; 7-453.
DR DIP; DIP-29937N; -.
DR IntAct; Q9Y265; 71.
DR MINT; MINT-1138777; -.
DR STRING; 9606.ENSP00000318297; -.
DR PhosphoSite; Q9Y265; -.
DR DMDM; 28201891; -.
DR OGP; Q9Y265; -.
DR REPRODUCTION-2DPAGE; Q9Y265; -.
DR SWISS-2DPAGE; Q9Y265; -.
DR PaxDb; Q9Y265; -.
DR PeptideAtlas; Q9Y265; -.
DR PRIDE; Q9Y265; -.
DR DNASU; 8607; -.
DR Ensembl; ENST00000322623; ENSP00000318297; ENSG00000175792.
DR Ensembl; ENST00000417360; ENSP00000393755; ENSG00000175792.
DR GeneID; 8607; -.
DR KEGG; hsa:8607; -.
DR UCSC; uc003ekh.3; human.
DR CTD; 8607; -.
DR GeneCards; GC03M127783; -.
DR HGNC; HGNC:10474; RUVBL1.
DR HPA; HPA019947; -.
DR HPA; HPA019948; -.
DR MIM; 603449; gene.
DR neXtProt; NX_Q9Y265; -.
DR PharmGKB; PA34887; -.
DR eggNOG; COG1224; -.
DR HOVERGEN; HBG054186; -.
DR InParanoid; Q9Y265; -.
DR KO; K04499; -.
DR OMA; NKVVSKY; -.
DR PhylomeDB; Q9Y265; -.
DR Reactome; REACT_115566; Cell Cycle.
DR ChiTaRS; RUVBL1; human.
DR EvolutionaryTrace; Q9Y265; -.
DR GeneWiki; RuvB-like_1; -.
DR GenomeRNAi; 8607; -.
DR NextBio; 32249; -.
DR PRO; PR:Q9Y265; -.
DR ArrayExpress; Q9Y265; -.
DR Bgee; Q9Y265; -.
DR CleanEx; HS_RUVBL1; -.
DR Genevestigator; Q9Y265; -.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005815; C:microtubule organizing center; 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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034080; P:CENP-A containing nucleosome assembly at centromere; TAS:Reactome.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0007067; P:mitosis; IEA:UniProtKB-KW.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR InterPro; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW ATP-binding; Cell cycle; Cell division; Chromatin regulator;
KW Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW DNA damage; DNA recombination; DNA repair; Growth regulation;
KW Helicase; Hydrolase; Membrane; Mitosis; Nucleotide-binding; Nucleus;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1 456 RuvB-like 1.
FT /FTId=PRO_0000165639.
FT NP_BIND 70 77 ATP (By similarity).
FT MOD_RES 453 453 N6-acetyllysine.
FT VAR_SEQ 374 386 IIKIRAQTEGINI -> VLSAAADPGQLAC (in
FT isoform 2).
FT /FTId=VSP_021387.
FT VAR_SEQ 387 456 Missing (in isoform 2).
FT /FTId=VSP_021388.
FT MUTAGEN 302 302 D->N: Abolishes ATPase activity;
FT inhibition of MYC- and CTNNB1-mediated
FT transformation.
FT CONFLICT 52 52 I -> T (in Ref. 12; BAD96283).
FT CONFLICT 145 145 N -> D (in Ref. 12; BAD96295).
FT CONFLICT 285 285 K -> R (in Ref. 8; ABF13334).
FT CONFLICT 353 353 D -> P (in Ref. 8; ABF13334).
FT HELIX 10 16
FT TURN 17 20
FT STRAND 28 30
FT STRAND 34 36
FT STRAND 39 41
FT HELIX 43 57
FT STRAND 65 69
FT STRAND 72 75
FT HELIX 76 87
FT STRAND 93 97
FT HELIX 98 101
FT STRAND 104 106
FT HELIX 108 118
FT STRAND 119 140
FT STRAND 157 163
FT STRAND 166 172
FT HELIX 174 182
FT STRAND 189 194
FT TURN 195 197
FT STRAND 200 206
FT STRAND 216 221
FT STRAND 228 239
FT HELIX 240 245
FT HELIX 278 288
FT STRAND 291 296
FT STRAND 298 303
FT HELIX 304 306
FT HELIX 309 318
FT STRAND 326 331
FT STRAND 334 337
FT STRAND 345 347
FT HELIX 352 355
FT STRAND 358 362
FT HELIX 368 382
FT HELIX 388 400
FT HELIX 403 408
FT HELIX 410 419
FT STRAND 423 425
FT HELIX 427 436
FT HELIX 440 448
SQ SEQUENCE 456 AA; 50228 MW; 6095ADE692B1482B CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK
//
MIM
603449
*RECORD*
*FIELD* NO
603449
*FIELD* TI
*603449 RUVB, E. COLI, HOMOLOG-LIKE 1; RUVBL1
;;NUCLEAR MATRIX PROTEIN 238; NMP238;;
read moreTATA BOX-BINDING PROTEIN-INTERACTING PROTEIN, 49-KD; TIP49;;
TBP-INTERACTING PROTEIN, 49-KD;;
PONTIN 52;;
PONTIN;;
ERYTHROCYTE CYTOSOLIC PROTEIN, 54-KD; ECP54
*FIELD* TX
CLONING
By 2-dimensional electrophoresis of nuclear matrix proteins from various
types of human cells, Holzmann et al. (1998) detected a common nuclear
matrix protein that they designated NMP238. Using a partial protein
sequence, they searched an EST database and identified a cDNA encoding
NMP238. The calculated molecular mass and pI of the predicted 456-amino
acid protein were close to the experimentally determined values of 54 kD
and 6.5. By immunofluorescence, Holzmann et al. (1998) determined that
NMP238 is found primarily in the nucleus, although it is also present in
the cytoplasm. The NMP238 staining pattern appeared as punctate signals
in both in situ prepared nuclear matrices and in the nucleoplasm of
whole cells. Northern blot and RNA dot blot analysis revealed that
NMP238 is expressed ubiquitously as an approximately 1.8-kb mRNA.
Bacterial RuvB proteins function as DNA helicases that promote branch
migration of Holliday junctions that form during genetic recombination.
Independently, Qiu et al. (1998) isolated NMP238 cDNAs, designating the
protein RUVBL1 (E. coli RuvB-like-1). They reported that RUVBL1 has
homology to bacterial RuvB proteins. The regions of homology contained,
among other motifs, Walker A and B motifs characteristic of DNA/RNA
helicases.
Makino et al. (1998) identified RUVBL1 as the human homolog of rat
TIP49, a 49-kD TATA box-binding protein (TBP; 600075)-interacting
protein. Rat and human TIP49 differ at only 1 amino acid position.
Bauer et al. (1998) demonstrated by immunofluorescence microscopy that
RUVBL1 is present in small dot-like structures in the nucleus but not in
nucleoli.
GENE FUNCTION
Qiu et al. (1998) found that RUVBL1 coimmunoprecipitated with several
cellular proteins and was present in the RNA polymerase II holoenzyme
complex purified over multiple chromatographic steps. Qiu et al. (1998)
identified 2 S. cerevisiae RuvB homologs, scRuvBL1 and scRuvBL2, which
share 70% and 42% protein sequence identity with RUVBL1, respectively.
They determined that scRuvBL1 is essential for viability in yeast.
Wood et al. (2000) used the MYC (190080) transactivation domain to
affinity purify tightly associated nuclear proteins. They identified 2
of these proteins as RUVBL1 and a novel related protein, RUVBL2
(604788). RUVBL1 and RUVBL2 are both highly conserved in evolution and
contain ATPase/helicase motifs. The authors showed that RUVBL1 and
RUVBL2 are complexed with MYC in vivo and that binding is dependent on a
MYC domain essential for oncogenic activity. A missense mutation in the
RUVBL1 ATPase motif acted as a dominant inhibitor of MYC oncogenic
activity but did not inhibit normal cell growth, indicating that
functional RUVBL1 protein is an essential mediator of MYC oncogenic
transformation. Wood et al. (2000) concluded that the RUVBL1 and RUVBL2
ATPase/helicase proteins represent a class of cofactors recruited by
transcriptional activation domains that function in diverse pathways.
Using the N-terminal 284 amino acids of beta-catenin (CTNNB1; 116806),
Bauer et al. (1998) identified RUVBL1, which they termed pontin-52, as a
52-kD binding partner of CTNNB1. Using binding analysis, they confirmed
that RUVBL1 serves as a bridge between CTNNB1 (residues 187-284) and TBP
as predicted by sequence analysis. Bauer et al. (1998) also observed
interaction between RUVBL1 and the CTNNB1-lymphoid enhancer-binding
factor-1 (LEF1; 153245) complex.
Hawley et al. (2001) identified TIP49 as a plasminogen (173350)-binding
protein on the surface of a monocytic cell line. Monocytic cells treated
with carboxypeptidase B (CPB1; 114852) lost the ability to bind and
activate plasminogen, and TIP49 was found to be the plasminogen-binding
protein altered by the CPB1 treatment. With use of recombinant rat TIP49
in an in vitro binding assay, Hawley et al. (2001) confirmed binding of
plasminogen to immobilized TIP49. They demonstrated activation of
TIP49-bound plasminogen by cleavage of a plasmin substrate.
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 RUVBL1 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 Ruvbl1,
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.
Makino et al. (1998) detected a high level of autoantibodies against
TIP49 in sera of patients with the autoimmune diseases
polymyositis/dermatomyositis and autoimmune hepatitis.
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 and reptin (RUVBL2) 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.
MAPPING
By fluorescence in situ hybridization, Qiu et al. (1998) mapped the
RUVBL1 gene to chromosome 3q21.
*FIELD* RF
1. Bauer, A.; Huber, O.; Kemler, R.: Pontin52, an interaction partner
of beta-catenin, binds to the TATA box binding protein. Proc. Nat.
Acad. Sci. 95: 14787-14792, 1998.
2. 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.
3. 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.
4. Hawley, S. B.; Tamura, T.; Miles, L. A.: Purification, cloning,
and characterization of a profibrinolytic plasminogen-binding protein,
TIP49a. J. Biol. Chem. 276: 179-186, 2001.
5. Holzmann, K.; Gerner, C.; Korosec, T.; Poltl, A.; Grimm, R.; Sauermann,
G.: Identification and characterization of the ubiquitously occurring
nuclear matrix protein NMP 238. Biochem. Biophys. Res. Commun. 252:
39-45, 1998.
6. Makino, Y.; Mimori, T.; Koike, C.; Kanemaki, M.; Kurokawa, Y.;
Inoue, S.; Kishimoto, T.; Tamura, T.: TIP49, homologous to the bacterial
DNA helicase RuvB, acts as an autoantigen in human. Biochem. Biophys.
Res. Commun. 245: 819-823, 1998.
7. Qiu, X.-B.; Lin, Y.-L.; Thome, K. C.; Pian, P.; Schlegel, B. P.;
Weremowicz, S.; Parvin, J. D.; Dutta, A.: An eukaryotic RuvB-like
protein (RUVBL1) essential for growth. J. Biol. Chem. 273: 27786-27793,
1998.
8. 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.
9. 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
Patricia A. Hartz - updated: 7/9/2002
Paul J. Converse - updated: 1/31/2001
Stylianos E. Antonarakis - updated: 4/4/2000
*FIELD* CD
Rebekah S. Rasooly: 1/19/1999
*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
carol: 7/9/2002
mgross: 2/28/2001
mcapotos: 2/7/2001
mcapotos: 1/31/2001
mgross: 4/4/2000
alopez: 1/19/1999
*RECORD*
*FIELD* NO
603449
*FIELD* TI
*603449 RUVB, E. COLI, HOMOLOG-LIKE 1; RUVBL1
;;NUCLEAR MATRIX PROTEIN 238; NMP238;;
read moreTATA BOX-BINDING PROTEIN-INTERACTING PROTEIN, 49-KD; TIP49;;
TBP-INTERACTING PROTEIN, 49-KD;;
PONTIN 52;;
PONTIN;;
ERYTHROCYTE CYTOSOLIC PROTEIN, 54-KD; ECP54
*FIELD* TX
CLONING
By 2-dimensional electrophoresis of nuclear matrix proteins from various
types of human cells, Holzmann et al. (1998) detected a common nuclear
matrix protein that they designated NMP238. Using a partial protein
sequence, they searched an EST database and identified a cDNA encoding
NMP238. The calculated molecular mass and pI of the predicted 456-amino
acid protein were close to the experimentally determined values of 54 kD
and 6.5. By immunofluorescence, Holzmann et al. (1998) determined that
NMP238 is found primarily in the nucleus, although it is also present in
the cytoplasm. The NMP238 staining pattern appeared as punctate signals
in both in situ prepared nuclear matrices and in the nucleoplasm of
whole cells. Northern blot and RNA dot blot analysis revealed that
NMP238 is expressed ubiquitously as an approximately 1.8-kb mRNA.
Bacterial RuvB proteins function as DNA helicases that promote branch
migration of Holliday junctions that form during genetic recombination.
Independently, Qiu et al. (1998) isolated NMP238 cDNAs, designating the
protein RUVBL1 (E. coli RuvB-like-1). They reported that RUVBL1 has
homology to bacterial RuvB proteins. The regions of homology contained,
among other motifs, Walker A and B motifs characteristic of DNA/RNA
helicases.
Makino et al. (1998) identified RUVBL1 as the human homolog of rat
TIP49, a 49-kD TATA box-binding protein (TBP; 600075)-interacting
protein. Rat and human TIP49 differ at only 1 amino acid position.
Bauer et al. (1998) demonstrated by immunofluorescence microscopy that
RUVBL1 is present in small dot-like structures in the nucleus but not in
nucleoli.
GENE FUNCTION
Qiu et al. (1998) found that RUVBL1 coimmunoprecipitated with several
cellular proteins and was present in the RNA polymerase II holoenzyme
complex purified over multiple chromatographic steps. Qiu et al. (1998)
identified 2 S. cerevisiae RuvB homologs, scRuvBL1 and scRuvBL2, which
share 70% and 42% protein sequence identity with RUVBL1, respectively.
They determined that scRuvBL1 is essential for viability in yeast.
Wood et al. (2000) used the MYC (190080) transactivation domain to
affinity purify tightly associated nuclear proteins. They identified 2
of these proteins as RUVBL1 and a novel related protein, RUVBL2
(604788). RUVBL1 and RUVBL2 are both highly conserved in evolution and
contain ATPase/helicase motifs. The authors showed that RUVBL1 and
RUVBL2 are complexed with MYC in vivo and that binding is dependent on a
MYC domain essential for oncogenic activity. A missense mutation in the
RUVBL1 ATPase motif acted as a dominant inhibitor of MYC oncogenic
activity but did not inhibit normal cell growth, indicating that
functional RUVBL1 protein is an essential mediator of MYC oncogenic
transformation. Wood et al. (2000) concluded that the RUVBL1 and RUVBL2
ATPase/helicase proteins represent a class of cofactors recruited by
transcriptional activation domains that function in diverse pathways.
Using the N-terminal 284 amino acids of beta-catenin (CTNNB1; 116806),
Bauer et al. (1998) identified RUVBL1, which they termed pontin-52, as a
52-kD binding partner of CTNNB1. Using binding analysis, they confirmed
that RUVBL1 serves as a bridge between CTNNB1 (residues 187-284) and TBP
as predicted by sequence analysis. Bauer et al. (1998) also observed
interaction between RUVBL1 and the CTNNB1-lymphoid enhancer-binding
factor-1 (LEF1; 153245) complex.
Hawley et al. (2001) identified TIP49 as a plasminogen (173350)-binding
protein on the surface of a monocytic cell line. Monocytic cells treated
with carboxypeptidase B (CPB1; 114852) lost the ability to bind and
activate plasminogen, and TIP49 was found to be the plasminogen-binding
protein altered by the CPB1 treatment. With use of recombinant rat TIP49
in an in vitro binding assay, Hawley et al. (2001) confirmed binding of
plasminogen to immobilized TIP49. They demonstrated activation of
TIP49-bound plasminogen by cleavage of a plasmin substrate.
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 RUVBL1 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 Ruvbl1,
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.
Makino et al. (1998) detected a high level of autoantibodies against
TIP49 in sera of patients with the autoimmune diseases
polymyositis/dermatomyositis and autoimmune hepatitis.
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 and reptin (RUVBL2) 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.
MAPPING
By fluorescence in situ hybridization, Qiu et al. (1998) mapped the
RUVBL1 gene to chromosome 3q21.
*FIELD* RF
1. Bauer, A.; Huber, O.; Kemler, R.: Pontin52, an interaction partner
of beta-catenin, binds to the TATA box binding protein. Proc. Nat.
Acad. Sci. 95: 14787-14792, 1998.
2. 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.
3. 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.
4. Hawley, S. B.; Tamura, T.; Miles, L. A.: Purification, cloning,
and characterization of a profibrinolytic plasminogen-binding protein,
TIP49a. J. Biol. Chem. 276: 179-186, 2001.
5. Holzmann, K.; Gerner, C.; Korosec, T.; Poltl, A.; Grimm, R.; Sauermann,
G.: Identification and characterization of the ubiquitously occurring
nuclear matrix protein NMP 238. Biochem. Biophys. Res. Commun. 252:
39-45, 1998.
6. Makino, Y.; Mimori, T.; Koike, C.; Kanemaki, M.; Kurokawa, Y.;
Inoue, S.; Kishimoto, T.; Tamura, T.: TIP49, homologous to the bacterial
DNA helicase RuvB, acts as an autoantigen in human. Biochem. Biophys.
Res. Commun. 245: 819-823, 1998.
7. Qiu, X.-B.; Lin, Y.-L.; Thome, K. C.; Pian, P.; Schlegel, B. P.;
Weremowicz, S.; Parvin, J. D.; Dutta, A.: An eukaryotic RuvB-like
protein (RUVBL1) essential for growth. J. Biol. Chem. 273: 27786-27793,
1998.
8. 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.
9. 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
Patricia A. Hartz - updated: 7/9/2002
Paul J. Converse - updated: 1/31/2001
Stylianos E. Antonarakis - updated: 4/4/2000
*FIELD* CD
Rebekah S. Rasooly: 1/19/1999
*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
carol: 7/9/2002
mgross: 2/28/2001
mcapotos: 2/7/2001
mcapotos: 1/31/2001
mgross: 4/4/2000
alopez: 1/19/1999