RUVB1_HUMAN
ID RUVB1_HUMAN Reviewed; 456 AA.
AC Q9Y265; B2R5S0; P82276; Q1KMR0; Q53HK5; Q53HL7; Q53Y27; Q9BSX9;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=RuvB-like 1 {ECO:0000305};
DE EC=3.6.4.12 {ECO:0000269|PubMed:17157868};
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 {ECO:0000312|HGNC:HGNC:10474};
GN Synonyms=INO80H, NMP238, TIP49, TIP49A;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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 nuclear
RT 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., Weremowicz S.,
RA 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 box
RT 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 of
RT ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic
RT proteins.";
RL Biochim. Biophys. Acta 1446:365-370(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182 AND
RP 184-201, FUNCTION, AND SUBCELLULAR LOCATION.
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., Daneva T.,
RA 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 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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT 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 project:
RT 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 IDENTIFICATION BY 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, MUTAGENESIS OF
RP ASP-302, AND FUNCTION.
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 IDENTIFICATION BY
RP MASS 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 TRRAP/TIP60-
RT 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, AND
RP IDENTIFICATION BY 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., Horikoshi M.,
RA 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 during
RT 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., Okazaki K.,
RA Morishita T., Tamura T.-A.;
RT "TIP49b, a new RuvB-like DNA helicase, is included in a complex together
RT 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., Aragnol D.,
RA Kemler R., Pradel J.;
RT "Pontin52 and reptin52 function as antagonistic regulators of beta-catenin
RT 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-Myc-
RT 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 T-cell
RT factor target gene induction via effects on chromatin 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 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, IDENTIFICATION BY MASS SPECTROMETRY,
RP AND FUNCTION.
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., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT 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 and
RT inhibits TCF-beta-catenin-mediated transcription.";
RL J. Cell Sci. 118:3117-3129(2005).
RN [27]
RP SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-302, AND ELECTRON
RP MICROSCOPY OF THE 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., 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 INTERACTION WITH PIH1D1.
RX PubMed=17636026; DOI=10.1128/mcb.01097-07;
RA McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.;
RT "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP
RT assembly.";
RL Mol. Cell. Biol. 27:6782-6793(2007).
RN [30]
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 [31]
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 G1/S
RT phase transition.";
RL Mol. Cell. Biol. 28:435-447(2008).
RN [32]
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 [33]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [34]
RP IDENTIFICATION IN THE R2TP COMPLEX.
RX PubMed=20864032; DOI=10.1016/j.molcel.2010.08.037;
RA Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S.,
RA Skehel J.M., de Lange T., Boulton S.J.;
RT "CK2 phospho-dependent binding of R2TP complex to TEL2 is essential for
RT mTOR and SMG1 stability.";
RL Mol. Cell 39:839-850(2010).
RN [35]
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., Buerckstuemmer T.,
RA 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 [36]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND FUNCTION.
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: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [37]
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [38]
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 pre-mRNA
RT splicing.";
RL Genes Dev. 27:1581-1595(2013).
RN [39]
RP INTERACTION WITH ITFG1.
RX PubMed=25437307; DOI=10.7554/elife.04449;
RA Kato M., Chou T.F., Yu C.Z., DeModena J., Sternberg P.W.;
RT "LINKIN, a new transmembrane protein necessary for cell adhesion.";
RL Elife 3:E04449-E04449(2014).
RN [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [41]
RP FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
RX PubMed=24463511; DOI=10.1038/nature12922;
RA Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K., Marek M.,
RA Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S., Romier C.,
RA Hamiche A.;
RT "ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
RL Nature 505:648-653(2014).
RN [42]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [44]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [45]
RP INTERACTION WITH WAC.
RX PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
RA David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M., Yamamoto S.,
RA Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z., Zhang S., Bellen H.J.;
RT "WAC regulates mTOR activity by acting as an adaptor for the TTT and
RT Pontin/Reptin complexes.";
RL Dev. Cell 36:139-151(2016).
RN [46]
RP INTERACTION WITH ZNHIT1; ZNHIT3; ZNHIT6 AND DDX59.
RX PubMed=28561026; DOI=10.1038/ncomms15615;
RA Cloutier P., Poitras C., Durand M., Hekmat O., Fiola-Masson E.,
RA Bouchard A., Faubert D., Chabot B., Coulombe B.;
RT "R2TP/Prefoldin-like component RUVBL1/RUVBL2 directly interacts with ZNHIT2
RT to regulate assembly of U5 small nuclear ribonucleoprotein.";
RL Nat. Commun. 8:15615-15615(2017).
RN [47]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-225 AND LYS-445, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [48]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599;
RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M.,
RA Gauthier M.S., Coulombe B.;
RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the
RT PAQosome.";
RL J. Proteome Res. 19:18-27(2020).
RN [49]
RP INTERACTION WITH NOPCHAP1, AND MUTAGENESIS OF LYS-76 AND GLU-303.
RX PubMed=33367824; DOI=10.1093/nar/gkaa1226;
RA Abel Y., Paiva A.C.F., Bizarro J., Chagot M.E., Santo P.E., Robert M.C.,
RA Quinternet M., Vandermoere F., Sousa P.M.F., Fort P., Charpentier B.,
RA Manival X., Bandeiras T.M., Bertrand E., Verheggen C.;
RT "NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2
RT during box C/D snoRNP biogenesis.";
RL Nucleic Acids Res. 49:1094-1113(2021).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF 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).
RN [51] {ECO:0007744|PDB:7AHO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.18 ANGSTROMS) IN COMPLEX WITH RUVBL2,
RP FUNCTION, SUBUNIT, INTERACTION WITH SMG1 AND DHX34, AND MUTAGENESIS OF
RP GLU-303.
RX PubMed=33205750; DOI=10.7554/elife.63042;
RA Lopez-Perrote A., Hug N., Gonzalez-Corpas A., Rodriguez C.F., Serna M.,
RA Garcia-Martin C., Boskovic J., Fernandez-Leiro R., Caceres J.F., Llorca O.;
RT "Regulation of RUVBL1-RUVBL2 AAA-ATPases by the nonsense-mediated mRNA
RT decay factor DHX34, as evidenced by Cryo-EM.";
RL Elife 9:0-0(2020).
CC -!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
CC dependent DNA helicase (3' to 5') activity; hexamerization is thought
CC to be critical for ATP hydrolysis and adjacent subunits in the ring-
CC like structure contribute to the ATPase activity (PubMed:17157868,
CC PubMed:33205750). Component of the NuA4 histone acetyltransferase
CC complex which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A
CC (PubMed:14966270). This modification may both alter nucleosome-DNA
CC interactions and promote interaction of the modified histones with
CC other proteins which positively regulate transcription
CC (PubMed:14966270). This complex may be required for the activation of
CC transcriptional programs associated with oncogene and proto-oncogene
CC mediated growth induction, tumor suppressor mediated growth arrest and
CC replicative senescence, apoptosis, and DNA repair (PubMed:14966270).
CC The NuA4 complex ATPase and helicase activities seem to be, at least in
CC part, contributed by the association of RUVBL1 and RUVBL2 with EP400.
CC NuA4 may also play a direct role in DNA repair when recruited to sites
CC of DNA damage (PubMed:14966270). Component of a SWR1-like complex that
CC specifically mediates the removal of histone H2A.Z/H2AZ1 from the
CC nucleosome (PubMed:24463511). Proposed core component of the chromatin
CC remodeling INO80 complex which exhibits DNA- and nucleosome-activated
CC ATPase activity and catalyzes ATP-dependent nucleosome sliding
CC (PubMed:16230350, PubMed:21303910). Plays an essential role in
CC oncogenic transformation by MYC and also modulates transcriptional
CC activation by the LEF1/TCF1-CTNNB1 complex (PubMed:10882073,
CC PubMed:16014379). Essential for cell proliferation (PubMed:14506706).
CC May be able to bind plasminogen at cell surface and enhance plasminogen
CC activation (PubMed:11027681). {ECO:0000269|PubMed:10882073,
CC ECO:0000269|PubMed:11027681, ECO:0000269|PubMed:14506706,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:16014379,
CC ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:17157868,
CC ECO:0000269|PubMed:21303910, ECO:0000269|PubMed:24463511,
CC ECO:0000269|PubMed:33205750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:17157868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:17157868};
CC -!- SUBUNIT: Forms homohexameric rings (PubMed:33205750). Can form a
CC dodecamer with RUVBL2 made of two stacked hexameric rings; however,
CC even though RUVBL1 and RUVBL2 are present in equimolar ratio, the
CC oligomeric status of each hexamer is not known (PubMed:33205750).
CC Oligomerization may regulate binding to nucleic acids and conversely,
CC binding to nucleic acids may affect the dodecameric assembly.
CC Interaction of the complex with DHX34 results in conformational changes
CC of the N-terminus of the RUVBL2 subunits, resulting in loss of
CC nucleotide binding ability and ATP hydrolysis of the complex
CC (PubMed:33205750). Interacts with the transcriptional activation domain
CC of MYC. Component of the RNA polymerase II holoenzyme complex. May also
CC act to bridge the LEF1/TCF1-CTNNB1 complex and TBP. Component of the
CC NuA4 histone acetyltransferase complex which contains the catalytic
CC subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP,
CC EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A,
CC MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6.
CC The NuA4 complex interacts with MYC and the adenovirus E1A protein.
CC RUVBL1 interacts with EP400. Component of a NuA4-related complex which
CC contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41.
CC Component of the BAF53 complex, at least composed of ACTL6A/BAF53A,
CC RUVBL1/TIP49, SMARCA2/BRM, and TRRAP/PAF400. Component of some MLL1/MLL
CC complex, at 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. Associates with alpha
CC and 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. Component of a SWR1-like
CC complex. Component of the R2TP complex composed at least of RUVBL1,
CC RUVBL2, RPAP3 and PIHD1 (PubMed:20864032). Component of the PAQosome
CC complex which is responsible for the biogenesis of several protein
CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2,
CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1
CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).
CC Interacts with PIH1D1 (PubMed:17636026). Interacts with ITFG1
CC (PubMed:25437307). Interacts with WAC; WAC positively regulates MTOR
CC activity by promoting the assembly of the TTT complex composed of
CC TELO2, TTI1 and TTI2 and the RUVBL complex composed of RUVBL1 and
CC RUVBL2 into the TTT-RUVBL complex which leads to the dimerization of
CC the mTORC1 complex and its subsequent activation (PubMed:26812014). The
CC RUVBL1/RUVBL2 complex interacts with ZNHIT1 (via HIT-type zinc finger),
CC ZNHIT3 (via HIT-type zinc finger), ZNHIT6 (via HIT-type zinc finger)
CC and DDX59/ZNHIT5 (via HIT-type zinc finger) in the presence of ADP
CC (PubMed:28561026). Interacts with NOPCHAP1; the interaction is direct
CC and disrupted upon ATP binding (PubMed:33367824). Interacts with SMG1
CC (PubMed:33205750). {ECO:0000269|PubMed:10428817,
CC ECO:0000269|PubMed:10882073, ECO:0000269|PubMed:10966108,
CC ECO:0000269|PubMed:11839798, ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14506706, ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16014379,
CC ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:17060327,
CC ECO:0000269|PubMed:17157868, ECO:0000269|PubMed:17636026,
CC ECO:0000269|PubMed:17761535, ECO:0000269|PubMed:17967892,
CC ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:19299493,
CC ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:23824326, ECO:0000269|PubMed:24463511,
CC ECO:0000269|PubMed:25437307, ECO:0000269|PubMed:26812014,
CC ECO:0000269|PubMed:28561026, ECO:0000269|PubMed:31738558,
CC ECO:0000269|PubMed:33205750, ECO:0000269|PubMed:33367824}.
CC -!- INTERACTION:
CC Q9Y265; P35222: CTNNB1; NbExp=3; IntAct=EBI-353675, EBI-491549;
CC Q9Y265; O60832: DKC1; NbExp=9; IntAct=EBI-353675, EBI-713091;
CC Q9Y265; O95905: ECD; NbExp=7; IntAct=EBI-353675, EBI-2557598;
CC Q9Y265; Q9Y283: INVS; NbExp=2; IntAct=EBI-353675, EBI-751472;
CC Q9Y265; Q15051: IQCB1; NbExp=2; IntAct=EBI-353675, EBI-2805823;
CC Q9Y265; Q92993: KAT5; NbExp=5; IntAct=EBI-353675, EBI-399080;
CC Q9Y265; O15259: NPHP1; NbExp=2; IntAct=EBI-353675, EBI-953828;
CC Q9Y265; Q7Z494: NPHP3; NbExp=2; IntAct=EBI-353675, EBI-2804263;
CC Q9Y265; O75161: NPHP4; NbExp=2; IntAct=EBI-353675, EBI-4281852;
CC Q9Y265; O75665: OFD1; NbExp=3; IntAct=EBI-353675, EBI-716327;
CC Q9Y265; Q9Y230: RUVBL2; NbExp=35; IntAct=EBI-353675, EBI-352939;
CC Q9Y265; O14746: TERT; NbExp=11; IntAct=EBI-353675, EBI-1772203;
CC Q9Y265; P04637: TP53; NbExp=10; IntAct=EBI-353675, EBI-366083;
CC Q9Y265; P63279: UBE2I; NbExp=3; IntAct=EBI-353675, EBI-80168;
CC Q9Y265; Q15906: VPS72; NbExp=7; IntAct=EBI-353675, EBI-399189;
CC Q9Y265; P25490: YY1; NbExp=6; IntAct=EBI-353675, EBI-765538;
CC Q9Y265; Q9UHR6: ZNHIT2; NbExp=6; IntAct=EBI-353675, EBI-2557592;
CC Q9Y265; G3I183: I79_017133; Xeno; NbExp=2; IntAct=EBI-353675, EBI-10890180;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm
CC {ECO:0000269|PubMed:11027681}. Membrane {ECO:0000269|PubMed:11027681}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
CC Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE26}. Note=Mainly
CC localized in the nucleus, associated with nuclear matrix or in the
CC nuclear cytosol, although it is also present in the cytoplasm and
CC associated with the cell membranes. In prophase and prometaphase it is
CC located at 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 through
CC metaphase and into telophase it is located close to the centrosome at
CC the early phase of tubulin polymerization. In anaphase it accumulates
CC at the zone of tubule interdigitation. In telophase it is found at
CC polar tubule overlap, and it reappears at the site of chromosomal
CC 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 detected
CC in sera of patients with autoimmune diseases such as
CC polymyositis/dermatomyosistis and autoimmune hepatitis.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL1ID44415ch3q21.html";
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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 CCDS; CCDS3047.1; -. [Q9Y265-1]
DR PIR; JE0334; JE0334.
DR RefSeq; NP_001306013.1; NM_001319084.1. [Q9Y265-2]
DR RefSeq; NP_003698.1; NM_003707.2. [Q9Y265-1]
DR PDB; 2C9O; X-ray; 2.20 A; A/B/C=1-456.
DR PDB; 2XSZ; X-ray; 3.00 A; A/B/C=2-126, A/B/C=234-456.
DR PDB; 5OAF; EM; 4.06 A; A/C/E=1-456.
DR PDB; 6FO1; EM; 3.57 A; A/B/C=1-456.
DR PDB; 6HTS; EM; 4.80 A; A/C/E=1-456.
DR PDB; 6IGM; EM; 4.00 A; A/C/E=1-456.
DR PDB; 6K0R; X-ray; 2.50 A; A/B/C/G/H/I=2-126, A/B/C/G/H/I=234-456.
DR PDB; 6QI8; EM; 3.75 A; A/B/C=1-456.
DR PDB; 6QI9; EM; 4.63 A; A/B/C=1-456.
DR PDB; 7AHO; EM; 4.18 A; A/B/C=1-456.
DR PDB; 7OLE; EM; 3.41 A; A/C/E=1-456.
DR PDB; 7P6X; EM; 4.10 A; A/B/C=1-456.
DR PDBsum; 2C9O; -.
DR PDBsum; 2XSZ; -.
DR PDBsum; 5OAF; -.
DR PDBsum; 6FO1; -.
DR PDBsum; 6HTS; -.
DR PDBsum; 6IGM; -.
DR PDBsum; 6K0R; -.
DR PDBsum; 6QI8; -.
DR PDBsum; 6QI9; -.
DR PDBsum; 7AHO; -.
DR PDBsum; 7OLE; -.
DR PDBsum; 7P6X; -.
DR AlphaFoldDB; Q9Y265; -.
DR SMR; Q9Y265; -.
DR BioGRID; 114166; 449.
DR ComplexPortal; CPX-6143; R2TP core co-chaperone complex.
DR ComplexPortal; CPX-6150; R2SP co-chaperone complex.
DR ComplexPortal; CPX-6152; R2SD co-chaperone complex.
DR ComplexPortal; CPX-6153; R2T co-chaperone complex.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; Q9Y265; -.
DR DIP; DIP-29937N; -.
DR IntAct; Q9Y265; 180.
DR MINT; Q9Y265; -.
DR STRING; 9606.ENSP00000318297; -.
DR BindingDB; Q9Y265; -.
DR ChEMBL; CHEMBL3259467; -.
DR GlyGen; Q9Y265; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y265; -.
DR MetOSite; Q9Y265; -.
DR PhosphoSitePlus; Q9Y265; -.
DR SwissPalm; Q9Y265; -.
DR BioMuta; RUVBL1; -.
DR DMDM; 28201891; -.
DR OGP; Q9Y265; -.
DR REPRODUCTION-2DPAGE; Q9Y265; -.
DR SWISS-2DPAGE; Q9Y265; -.
DR CPTAC; CPTAC-268; -.
DR CPTAC; CPTAC-269; -.
DR EPD; Q9Y265; -.
DR jPOST; Q9Y265; -.
DR MassIVE; Q9Y265; -.
DR MaxQB; Q9Y265; -.
DR PaxDb; Q9Y265; -.
DR PeptideAtlas; Q9Y265; -.
DR PRIDE; Q9Y265; -.
DR ProteomicsDB; 85669; -. [Q9Y265-1]
DR ProteomicsDB; 85670; -. [Q9Y265-2]
DR Antibodypedia; 17283; 387 antibodies from 34 providers.
DR DNASU; 8607; -.
DR Ensembl; ENST00000322623.10; ENSP00000318297.5; ENSG00000175792.12. [Q9Y265-1]
DR Ensembl; ENST00000643444.2; ENSP00000494621.1; ENSG00000284901.2. [Q9Y265-1]
DR GeneID; 8607; -.
DR KEGG; hsa:8607; -.
DR MANE-Select; ENST00000322623.10; ENSP00000318297.5; NM_003707.3; NP_003698.1.
DR UCSC; uc003ekh.4; human. [Q9Y265-1]
DR CTD; 8607; -.
DR DisGeNET; 8607; -.
DR GeneCards; RUVBL1; -.
DR HGNC; HGNC:10474; RUVBL1.
DR HPA; ENSG00000175792; Low tissue specificity.
DR MIM; 603449; gene.
DR neXtProt; NX_Q9Y265; -.
DR OpenTargets; ENSG00000175792; -.
DR PharmGKB; PA34887; -.
DR VEuPathDB; HostDB:ENSG00000175792; -.
DR eggNOG; KOG1942; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_1_1_1; -.
DR InParanoid; Q9Y265; -.
DR OMA; VIYVEAN; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; Q9Y265; -.
DR TreeFam; TF300457; -.
DR PathwayCommons; Q9Y265; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR SignaLink; Q9Y265; -.
DR BioGRID-ORCS; 8607; 730 hits in 1067 CRISPR screens.
DR ChiTaRS; RUVBL1; human.
DR EvolutionaryTrace; Q9Y265; -.
DR GeneWiki; RuvB-like_1; -.
DR GenomeRNAi; 8607; -.
DR Pharos; Q9Y265; Tbio.
DR PRO; PR:Q9Y265; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y265; protein.
DR Bgee; ENSG00000175792; Expressed in right uterine tube and 98 other tissues.
DR ExpressionAtlas; Q9Y265; baseline and differential.
DR Genevisible; Q9Y265; HS.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
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:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0097255; C:R2TP complex; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
DR GO; GO:0043531; F:ADP binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IDA:UniProtKB.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0017025; F:TBP-class protein binding; IDA:UniProtKB.
DR GO; GO:0001094; F:TFIID-class transcription factor complex binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IBA:GO_Central.
DR GO; GO:0043486; P:histone exchange; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; IDA:UniProtKB.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA:ComplexPortal.
DR GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; HMP:BHF-UCL.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR Gene3D; 2.40.50.360; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR027238; RuvB-like.
DR InterPro; IPR041048; RuvB-like_C.
DR InterPro; IPR037938; RUVBL1.
DR InterPro; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF6; PTHR11093:SF6; 1.
DR Pfam; PF06068; TIP49; 1.
DR Pfam; PF17856; TIP49_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding;
KW Cell cycle; Cell division; Chromatin regulator; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
KW Growth regulation; Helicase; Hydrolase; Isopeptide bond; Membrane; Mitosis;
KW Nucleotide-binding; Nucleus; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..456
FT /note="RuvB-like 1"
FT /id="PRO_0000165639"
FT BINDING 70..77
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 453
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 2
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 225
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 445
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 374..386
FT /note="IIKIRAQTEGINI -> VLSAAADPGQLAC (in isoform 2)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_021387"
FT VAR_SEQ 387..456
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_021388"
FT MUTAGEN 76
FT /note="K->M: No effect on interaction with NOPCHAP1."
FT /evidence="ECO:0000269|PubMed:33367824"
FT MUTAGEN 302
FT /note="D->N: Abolishes ATPase activity; inhibition of
FT MYC- and CTNNB1-mediated transformation."
FT /evidence="ECO:0000269|PubMed:10882073,
FT ECO:0000269|PubMed:14695187, ECO:0000269|PubMed:17060327,
FT ECO:0000269|PubMed:17157868"
FT MUTAGEN 303
FT /note="E->Q: Reduces ATPase activity. Decreases interaction
FT with NOPCHAP1. No effect on formation of RUVBL1-RUVBL2
FT heteromeric complex."
FT /evidence="ECO:0000269|PubMed:33205750,
FT ECO:0000269|PubMed:33367824"
FT CONFLICT 52
FT /note="I -> T (in Ref. 12; BAD96283)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="N -> D (in Ref. 12; BAD96295)"
FT /evidence="ECO:0000305"
FT CONFLICT 285
FT /note="K -> R (in Ref. 8; ABF13334)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="D -> P (in Ref. 8; ABF13334)"
FT /evidence="ECO:0000305"
FT HELIX 10..16
FT /evidence="ECO:0007829|PDB:2C9O"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:2XSZ"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 43..57
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 65..69
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:2XSZ"
FT HELIX 76..87
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 98..101
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 104..106
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 108..118
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 119..140
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 157..163
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 189..194
FT /evidence="ECO:0007829|PDB:2C9O"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:7OLE"
FT STRAND 216..221
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 228..239
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 240..245
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 298..303
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 304..306
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 309..318
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 321..323
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 326..331
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 334..337
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 345..347
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 352..355
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 358..362
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 368..382
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 388..400
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 403..408
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 410..419
FT /evidence="ECO:0007829|PDB:2C9O"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:2C9O"
FT HELIX 440..448
FT /evidence="ECO:0007829|PDB:2C9O"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:7OLE"
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
