RUVB2_HUMAN
ID RUVB2_HUMAN Reviewed; 463 AA.
AC Q9Y230; B3KQ59; E7ETE5; Q6FIB9; Q6PK27; Q9Y361;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 235.
DE RecName: Full=RuvB-like 2;
DE EC=3.6.4.12 {ECO:0000269|PubMed:10428817, ECO:0000269|PubMed:17157868};
DE AltName: Full=48 kDa TATA box-binding protein-interacting protein;
DE Short=48 kDa TBP-interacting protein;
DE AltName: Full=51 kDa erythrocyte cytosolic protein;
DE Short=ECP-51;
DE AltName: Full=INO80 complex subunit J;
DE AltName: Full=Repressing pontin 52;
DE Short=Reptin 52;
DE AltName: Full=TIP49b;
DE AltName: Full=TIP60-associated protein 54-beta;
DE Short=TAP54-beta;
GN Name=RUVBL2; Synonyms=INO80J, TIP48, TIP49B; ORFNames=CGI-46;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 72-83;
RP 131-144; 212-223; 369-372 AND 440-457.
RC TISSUE=Bone marrow;
RX PubMed=10524211; DOI=10.1016/s0167-4781(99)00104-9;
RA Salzer U., Kubicek M., Prohaska R.;
RT "Isolation, molecular characterization, and tissue-specific expression of
RT ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid cytosolic
RT proteins.";
RL Biochim. Biophys. Acta 1446:365-370(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RUVBL1, FUNCTION,
RP CATALYTIC ACTIVITY, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10428817; DOI=10.1074/jbc.274.32.22437;
RA Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A., 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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=10998447; DOI=10.1016/s0003-3995(00)01016-9;
RA Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M.,
RA Vodovar N., Vidaud D., Vidaud M., Bieche I.;
RT "Human TIP49b/RUVBL2 gene: genomic structure, expression pattern, physical
RT link to the human CGB/LHB gene cluster on chromosome 19q13.3.";
RL Ann. Genet. 43:69-74(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal liver;
RX PubMed=11080158; DOI=10.1093/emboj/19.22.6121;
RA Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U., 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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 73-83; 116-124;
RP 237-253 AND 254-269, INTERACTION WITH MYC, 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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Embryo, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [13]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [14]
RP PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177; 237-269;
RP 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION
RP AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Gottlieb E.;
RL Submitted (MAR-2008) to UniProtKB.
RN [15]
RP PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427, IDENTIFICATION IN
RP THE NUA4 COMPLEX, AND 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 [16]
RP PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365;
RP 418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, AND 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 INTERACTION WITH ATF2, AND FUNCTION.
RX PubMed=11713276; DOI=10.1128/mcb.21.24.8398-8413.2001;
RA Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.;
RT "TIP49b, a regulator of activating transcription factor 2 response to
RT stress and DNA damage.";
RL Mol. Cell. Biol. 21:8398-8413(2001).
RN [18]
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 [19]
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 [20]
RP IDENTIFICATION IN INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP 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 [21]
RP INTERACTION WITH HINT1, AND FUNCTION.
RX PubMed=16014379; DOI=10.1242/jcs.02437;
RA Weiske J., Huber O.;
RT "The histidine triad protein Hint1 interacts with Pontin and Reptin and
RT inhibits TCF-beta-catenin-mediated transcription.";
RL J. Cell Sci. 118:3117-3129(2005).
RN [22]
RP SUBUNIT, FUNCTION, MUTAGENESIS OF ASP-299, AND ELECTRON MICROSCOPY OF THE
RP RUVBL1-RUVBL2 HETEROMER.
RX PubMed=17157868; DOI=10.1016/j.jmb.2006.11.030;
RA Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.;
RT "Dodecameric structure and ATPase activity of the human TIP48/TIP49
RT complex.";
RL J. Mol. Biol. 366:179-192(2007).
RN [23]
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 [24]
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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [26]
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 [27]
RP INTERACTION WITH APPL1 AND APPL2.
RX PubMed=19433865; DOI=10.1074/jbc.m109.007237;
RA Rashid S., Pilecka I., Torun A., Olchowik M., Bielinska B., Miaczynska M.;
RT "Endosomal adaptor proteins APPL1 and APPL2 are novel activators of beta-
RT catenin/TCF-mediated transcription.";
RL J. Biol. Chem. 284:18115-18128(2009).
RN [28]
RP INTERACTION WITH TELO2.
RX PubMed=20801936; DOI=10.1101/gad.1956410;
RA Takai H., Xie Y., de Lange T., Pavletich N.P.;
RT "Tel2 structure and function in the Hsp90-dependent maturation of mTOR and
RT ATR complexes.";
RL Genes Dev. 24:2019-2030(2010).
RN [29]
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 [30]
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 [31]
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 [32]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [33]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [34]
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 [35]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [36]
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 [37]
RP FUNCTION.
RX PubMed=25652260; DOI=10.15252/embr.201439123;
RA Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M.,
RA Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J.,
RA Palladino F., Dupuy D., Chevet E.;
RT "Genome-wide screen identifies a novel p97/CDC-48-dependent pathway
RT regulating ER-stress-induced gene transcription.";
RL EMBO Rep. 16:332-340(2015).
RN [38]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [39]
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 [40]
RP FUNCTION, AND INTERACTION WITH ZNHIT1; ZNHIT2; 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 [41]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-444 AND LYS-456, 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 [42]
RP INTERACTION WITH ZMYND10.
RX PubMed=29601588; DOI=10.1371/journal.pgen.1007316;
RA Cho K.J., Noh S.H., Han S.M., Choi W.I., Kim H.Y., Yu S., Lee J.S.,
RA Rim J.H., Lee M.G., Hildebrandt F., Gee H.Y.;
RT "ZMYND10 stabilizes intermediate chain proteins in the cytoplasmic pre-
RT assembly of dynein arms.";
RL PLoS Genet. 14:E1007316-E1007316(2018).
RN [43]
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 [44]
RP INTERACTION WITH NOPCHAP1, AND MUTAGENESIS OF LYS-83 AND GLU-300.
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 [45]
RP STRUCTURE BY NMR OF 132-213.
RG Mycobacterium tuberculosis structural genomics consortium (TB);
RT "Solution structure of RSGI RUH-039, a fragment of C-terminal domain of
RT RuvB-like 2 from human cDNA.";
RL Submitted (NOV-2005) to the PDB data bank.
RN [46] {ECO:0007744|PDB:7AHO}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.18 ANGSTROMS) IN COMPLEX WITH RUVBL1,
RP SUBUNIT, INTERACTION WITH SMG1 AND DHX34, AND MUTAGENESIS OF GLU-300.
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 (5' to 3') 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:10428817,
CC PubMed:17157868, PubMed:33205750). Component of the NuA4 histone
CC acetyltransferase complex which is involved in transcriptional
CC activation of select genes principally by acetylation of nucleosomal
CC histones H4 and H2A (PubMed:14966270). This modification may both alter
CC nucleosome -DNA interactions and promote interaction of the modified
CC histones with 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 (PubMed:14966270). NuA4 may also play a direct role in DNA repair when
CC recruited to sites of DNA damage (PubMed:14966270). Component of a
CC SWR1-like complex that specifically mediates the removal of histone
CC H2A.Z/H2AZ1 from the nucleosome (PubMed:24463511). Proposed core
CC component of the chromatin remodeling INO80 complex which exhibits
CC DNA- and nucleosome-activated ATPase activity and catalyzes ATP-
CC dependent nucleosome sliding (PubMed:16230350, PubMed:21303910). Plays
CC an essential role in oncogenic transformation by MYC and also modulates
CC transcriptional activation by the LEF1/TCF1-CTNNB1 complex
CC (PubMed:10882073, PubMed:16014379). May also inhibit the
CC transcriptional activity of ATF2 (PubMed:11713276). Involved in the
CC endoplasmic reticulum (ER)-associated degradation (ERAD) pathway where
CC it negatively regulates expression of ER stress response genes
CC (PubMed:25652260). May play a role in regulating the composition of the
CC U5 snRNP complex (PubMed:28561026). {ECO:0000269|PubMed:10428817,
CC ECO:0000269|PubMed:10882073, ECO:0000269|PubMed:11713276,
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:25652260, ECO:0000269|PubMed:28561026,
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:10428817, ECO:0000269|PubMed:17157868};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000305|PubMed:10428817};
CC -!- SUBUNIT: Forms homohexameric rings (PubMed:33205750). Can form a
CC dodecamer with RUVBL1 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. Interacts With ATF2. Component of the RNA polymerase II
CC holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1 complex
CC and TBP. Component of the NuA4 histone acetyltransferase complex which
CC contains the catalytic subunit KAT5/TIP60 and the subunits EP400,
CC TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2,
CC ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP,
CC YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC
CC and the adenovirus E1A protein. RUVBL2 interacts with EP400. Component
CC of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP,
CC BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Interacts with NPAT. Component
CC of the chromatin-remodeling INO80 complex; specifically part of a
CC complex module associated with the helicase ATP-binding and the
CC helicase C-terminal domain of INO80. 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. Interacts with IGHMBP2.
CC Interacts with TELO2. Interacts with HINT1. 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 ITFG1 (PubMed:25437307). Interacts with ZMYND10
CC (PubMed:29601588). 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).
CC Forms a complex with APPL1 and APPL2 (PubMed:19433865). Interacts with
CC ZNHIT2 (via HIT-type zinc finger) in the presence of ATP or ADP; shows
CC a stronger interaction in the presence of ADP (PubMed:28561026). 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:11713276, ECO:0000269|PubMed:12963728,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15960975,
CC ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:17157868, ECO:0000269|PubMed:17967892,
CC ECO:0000269|PubMed:18026119, ECO:0000269|PubMed:19299493,
CC ECO:0000269|PubMed:19433865, ECO:0000269|PubMed:20801936,
CC ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:21303910,
CC ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:25437307,
CC ECO:0000269|PubMed:26812014, ECO:0000269|PubMed:28561026,
CC ECO:0000269|PubMed:29601588, ECO:0000269|PubMed:31738558,
CC ECO:0000269|PubMed:33205750, ECO:0000269|PubMed:33367824, ECO:0000305}.
CC -!- INTERACTION:
CC Q9Y230; Q8IW40: CCDC103; NbExp=3; IntAct=EBI-352939, EBI-10261970;
CC Q9Y230; Q9UDY4: DNAJB4; NbExp=3; IntAct=EBI-352939, EBI-356960;
CC Q9Y230; Q9BVM2: DPCD; NbExp=10; IntAct=EBI-352939, EBI-749988;
CC Q9Y230; Q96L91: EP400; NbExp=2; IntAct=EBI-352939, EBI-399163;
CC Q9Y230; Q8TBB1: LNX1; NbExp=6; IntAct=EBI-352939, EBI-739832;
CC Q9Y230; Q9Y265: RUVBL1; NbExp=35; IntAct=EBI-352939, EBI-353675;
CC Q9Y230; Q9Y230: RUVBL2; NbExp=3; IntAct=EBI-352939, EBI-352939;
CC Q9Y230; P25490: YY1; NbExp=8; IntAct=EBI-352939, EBI-765538;
CC Q9Y230; Q8BPA8: Dpcd; Xeno; NbExp=2; IntAct=EBI-352939, EBI-26898155;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm. Cytoplasm.
CC Membrane. Dynein axonemal particle {ECO:0000250|UniProtKB:Q9DE27}.
CC Note=Mainly localized in the nucleus, associated with nuclear matrix or
CC in the nuclear cytosol. Although it is also present in the cytoplasm
CC and associated with the cell membranes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y230-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y230-2; Sequence=VSP_056584;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in testis
CC and thymus. {ECO:0000269|PubMed:10428817}.
CC -!- DOMAIN: The C-terminal domain is required for association with ATF2.
CC -!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD34041.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH08355.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RUVBL2ID42185ch19q13.html";
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DR EMBL; Y18417; CAB46270.1; -; mRNA.
DR EMBL; AB024301; BAA76708.1; -; mRNA.
DR EMBL; AF155138; AAD38073.1; -; mRNA.
DR EMBL; AF124607; AAF87087.1; -; mRNA.
DR EMBL; AF151804; AAD34041.1; ALT_FRAME; mRNA.
DR EMBL; AL136743; CAB66677.1; -; mRNA.
DR EMBL; AK057498; BAG51921.1; -; mRNA.
DR EMBL; AK074542; BAC11048.1; -; mRNA.
DR EMBL; CR533507; CAG38538.1; -; mRNA.
DR EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471177; EAW52426.1; -; Genomic_DNA.
DR EMBL; CH471177; EAW52430.1; -; Genomic_DNA.
DR EMBL; BC000428; AAH00428.1; -; mRNA.
DR EMBL; BC004531; AAH04531.1; -; mRNA.
DR EMBL; BC008355; AAH08355.1; ALT_FRAME; mRNA.
DR CCDS; CCDS42588.1; -. [Q9Y230-1]
DR PIR; T46313; T46313.
DR RefSeq; NP_001308120.1; NM_001321191.1. [Q9Y230-2]
DR RefSeq; NP_006657.1; NM_006666.2. [Q9Y230-1]
DR RefSeq; XP_011524632.1; XM_011526330.1. [Q9Y230-2]
DR PDB; 2CQA; NMR; -; A=132-213.
DR PDB; 2XSZ; X-ray; 3.00 A; D/E/F=2-133, D/E/F=238-463.
DR PDB; 3UK6; X-ray; 2.95 A; A/B/C/D/E/F/G/H/I/J/K/L=1-132, A/B/C/D/E/F/G/H/I/J/K/L=239-463.
DR PDB; 5OAF; EM; 4.06 A; B/D/F=1-463.
DR PDB; 6FO1; EM; 3.57 A; D/E/F=1-463.
DR PDB; 6H7X; X-ray; 2.89 A; A=1-463.
DR PDB; 6HTS; EM; 4.80 A; B/D/F=1-463.
DR PDB; 6IGM; EM; 4.00 A; B/D/F=1-463.
DR PDB; 6K0R; X-ray; 2.50 A; D/E/F/J/K/L=1-133, D/E/F/J/K/L=238-463.
DR PDB; 6QI8; EM; 3.75 A; D/E/F=1-463.
DR PDB; 6QI9; EM; 4.63 A; D/E/F=1-463.
DR PDB; 7AHO; EM; 4.18 A; D/E/F=1-463.
DR PDB; 7OLE; EM; 3.41 A; B/D/F=1-463.
DR PDB; 7P6X; EM; 4.10 A; D/E/F=1-463.
DR PDBsum; 2CQA; -.
DR PDBsum; 2XSZ; -.
DR PDBsum; 3UK6; -.
DR PDBsum; 5OAF; -.
DR PDBsum; 6FO1; -.
DR PDBsum; 6H7X; -.
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; Q9Y230; -.
DR SMR; Q9Y230; -.
DR BioGRID; 116067; 438.
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; Q9Y230; -.
DR DIP; DIP-28153N; -.
DR IntAct; Q9Y230; 206.
DR MINT; Q9Y230; -.
DR STRING; 9606.ENSP00000473172; -.
DR ChEMBL; CHEMBL2062349; -.
DR DrugBank; DB04216; Quercetin.
DR GlyGen; Q9Y230; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y230; -.
DR MetOSite; Q9Y230; -.
DR PhosphoSitePlus; Q9Y230; -.
DR SwissPalm; Q9Y230; -.
DR BioMuta; RUVBL2; -.
DR DMDM; 28201890; -.
DR REPRODUCTION-2DPAGE; IPI00009104; -.
DR CPTAC; CPTAC-270; -.
DR CPTAC; CPTAC-271; -.
DR EPD; Q9Y230; -.
DR jPOST; Q9Y230; -.
DR MassIVE; Q9Y230; -.
DR MaxQB; Q9Y230; -.
DR PaxDb; Q9Y230; -.
DR PeptideAtlas; Q9Y230; -.
DR PRIDE; Q9Y230; -.
DR ProteomicsDB; 3549; -.
DR ProteomicsDB; 85619; -. [Q9Y230-1]
DR Antibodypedia; 3244; 429 antibodies from 36 providers.
DR DNASU; 10856; -.
DR Ensembl; ENST00000595090.6; ENSP00000473172.1; ENSG00000183207.14. [Q9Y230-1]
DR GeneID; 10856; -.
DR KEGG; hsa:10856; -.
DR MANE-Select; ENST00000595090.6; ENSP00000473172.1; NM_006666.3; NP_006657.1.
DR UCSC; uc002plr.2; human. [Q9Y230-1]
DR CTD; 10856; -.
DR DisGeNET; 10856; -.
DR GeneCards; RUVBL2; -.
DR HGNC; HGNC:10475; RUVBL2.
DR HPA; ENSG00000183207; Low tissue specificity.
DR MIM; 604788; gene.
DR neXtProt; NX_Q9Y230; -.
DR OpenTargets; ENSG00000183207; -.
DR PharmGKB; PA34888; -.
DR VEuPathDB; HostDB:ENSG00000183207; -.
DR eggNOG; KOG2680; Eukaryota.
DR GeneTree; ENSGT00940000153556; -.
DR HOGENOM; CLU_028311_4_0_1; -.
DR InParanoid; Q9Y230; -.
DR OMA; YDMGAKM; -.
DR OrthoDB; 752343at2759; -.
DR PhylomeDB; Q9Y230; -.
DR TreeFam; TF300469; -.
DR PathwayCommons; Q9Y230; -.
DR Reactome; R-HSA-171319; Telomere Extension By Telomerase.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR SignaLink; Q9Y230; -.
DR BioGRID-ORCS; 10856; 806 hits in 1051 CRISPR screens.
DR ChiTaRS; RUVBL2; human.
DR EvolutionaryTrace; Q9Y230; -.
DR GeneWiki; RUVBL2; -.
DR GenomeRNAi; 10856; -.
DR Pharos; Q9Y230; Tbio.
DR PRO; PR:Q9Y230; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9Y230; protein.
DR Bgee; ENSG00000183207; Expressed in left testis and 200 other tissues.
DR ExpressionAtlas; Q9Y230; baseline and differential.
DR Genevisible; Q9Y230; HS.
DR GO; GO:0005813; C:centrosome; IDA:HPA.
DR GO; GO:0101031; C:chaperone complex; IPI:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0120293; C:dynein axonemal particle; ISS:UniProtKB.
DR GO; GO:0000791; C:euchromatin; IDA: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: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:0008013; F:beta-catenin binding; IDA:UniProtKB.
DR GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0140585; F:promoter-enhancer loop anchoring activity; IMP:GO_Central.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; 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:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
DR GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
DR GO; GO:0006281; P:DNA repair; TAS:ProtInc.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
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:0090090; P:negative 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:0035066; P:positive regulation of histone acetylation; IMP:UniProtKB.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0006457; P:protein folding; TAS:ProtInc.
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: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; IPR042487; RuvBL1/2_DNA/RNA_bd_dom.
DR InterPro; IPR037942; RUVBL2.
DR InterPro; IPR010339; TIP49_P-loop.
DR PANTHER; PTHR11093; PTHR11093; 1.
DR PANTHER; PTHR11093:SF2; PTHR11093:SF2; 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 Chromatin regulator; Cytoplasm; Direct protein sequencing; DNA damage;
KW DNA recombination; DNA repair; Growth regulation; Helicase; Hydrolase;
KW Isopeptide bond; Membrane; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.14,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:22814378,
FT ECO:0007744|PubMed:25944712"
FT CHAIN 2..463
FT /note="RuvB-like 2"
FT /id="PRO_0000165644"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.14, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 9
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 444
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 456
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056584"
FT MUTAGEN 83
FT /note="K->M: No effect on interaction with NOPCHAP1."
FT /evidence="ECO:0000269|PubMed:33367824"
FT MUTAGEN 299
FT /note="D->N: Abolishes ATPase activity."
FT /evidence="ECO:0000269|PubMed:17157868"
FT MUTAGEN 300
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 214
FT /note="D -> N (in Ref. 6; AAD34041)"
FT /evidence="ECO:0000305"
FT CONFLICT 257..258
FT /note="FL -> YV (in Ref. 5; AA sequence)"
FT /evidence="ECO:0000305"
FT TURN 19..22
FT /evidence="ECO:0007829|PDB:3UK6"
FT TURN 24..27
FT /evidence="ECO:0007829|PDB:2XSZ"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:6K0R"
FT TURN 66..70
FT /evidence="ECO:0007829|PDB:6H7X"
FT STRAND 72..76
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 83..92
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 96..98
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 117..125
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 127..130
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 132..138
FT /evidence="ECO:0007829|PDB:7OLE"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:7OLE"
FT STRAND 152..156
FT /evidence="ECO:0007829|PDB:2CQA"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:6H7X"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:6H7X"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:6H7X"
FT STRAND 191..194
FT /evidence="ECO:0007829|PDB:6H7X"
FT TURN 197..200
FT /evidence="ECO:0007829|PDB:2CQA"
FT STRAND 201..206
FT /evidence="ECO:0007829|PDB:2CQA"
FT STRAND 232..239
FT /evidence="ECO:0007829|PDB:7OLE"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 244..250
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 259..262
FT /evidence="ECO:0007829|PDB:6H7X"
FT HELIX 270..286
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 295..299
FT /evidence="ECO:0007829|PDB:6K0R"
FT TURN 300..302
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 306..316
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 323..329
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 348..351
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 354..358
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 364..375
FT /evidence="ECO:0007829|PDB:6K0R"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 384..396
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 399..415
FT /evidence="ECO:0007829|PDB:6K0R"
FT STRAND 419..421
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 424..432
FT /evidence="ECO:0007829|PDB:6K0R"
FT HELIX 436..449
FT /evidence="ECO:0007829|PDB:6K0R"
SQ SEQUENCE 463 AA; 51157 MW; 54C78E9C587D975A CRC64;
MATVTATTKV PEIRDVTRIE RIGAHSHIRG LGLDDALEPR QASQGMVGQL AARRAAGVVL
EMIREGKIAG RAVLIAGQPG TGKTAIAMGM AQALGPDTPF TAIAGSEIFS LEMSKTEALT
QAFRRSIGVR IKEETEIIEG EVVEIQIDRP ATGTGSKVGK LTLKTTEMET IYDLGTKMIE
SLTKDKVQAG DVITIDKATG KISKLGRSFT RARDYDAMGS QTKFVQCPDG ELQKRKEVVH
TVSLHEIDVI NSRTQGFLAL FSGDTGEIKS EVREQINAKV AEWREEGKAE IIPGVLFIDE
VHMLDIESFS FLNRALESDM APVLIMATNR GITRIRGTSY QSPHGIPIDL LDRLLIVSTT
PYSEKDTKQI LRIRCEEEDV EMSEDAYTVL TRIGLETSLR YAIQLITAAS LVCRKRKGTE
VQVDDIKRVY SLFLDESRST QYMKEYQDAF LFNELKGETM DTS
