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 27-MAR-2024, entry version 244. 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="https://atlasgeneticsoncology.org/gene/42185/RUVBL2"; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. 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 PDB; 7ZI4; EM; 3.20 A; B/D/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 PDBsum; 7ZI4; -. DR AlphaFoldDB; Q9Y230; -. DR EMDB; EMD-11789; -. DR EMDB; EMD-12979; -. DR EMDB; EMD-13233; -. DR EMDB; EMD-14737; -. DR EMDB; EMD-3773; -. DR EMDB; EMD-3954; -. DR EMDB; EMD-4287; -. DR EMDB; EMD-4289; -. DR EMDB; EMD-4290; -. DR EMDB; EMD-4291; -. DR EMDB; EMD-4552; -. DR EMDB; EMD-4553; -. DR EMDB; EMD-4554; -. DR EMDB; EMD-4555; -. DR EMDB; EMD-4556; -. DR EMDB; EMD-4557; -. DR EMDB; EMD-9668; -. DR SASBDB; Q9Y230; -. DR SMR; Q9Y230; -. DR BioGRID; 116067; 612. 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; 210. DR MINT; Q9Y230; -. DR STRING; 9606.ENSP00000473172; -. DR BindingDB; Q9Y230; -. DR ChEMBL; CHEMBL2062349; -. DR DrugBank; DB04216; Quercetin. DR GlyGen; Q9Y230; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000473172; -. DR PeptideAtlas; Q9Y230; -. DR ProteomicsDB; 3549; -. DR ProteomicsDB; 85619; -. [Q9Y230-1] DR Pumba; Q9Y230; -. DR Antibodypedia; 3244; 489 antibodies from 36 providers. DR DNASU; 10856; -. DR Ensembl; ENST00000595090.6; ENSP00000473172.1; ENSG00000183207.15. [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 AGR; HGNC:10475; -. 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; NRGISRI; -. DR OrthoDB; 5479950at2759; -. 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 SIGNOR; Q9Y230; -. DR BioGRID-ORCS; 10856; 842 hits in 1140 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 202 other cell types or tissues. DR ExpressionAtlas; Q9Y230; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. 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:0101031; C:protein folding chaperone complex; IPI:ComplexPortal. 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:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:UniProtKB. DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:ComplexPortal. 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; ISO:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB. DR GO; GO:0006457; P:protein folding; TAS:ProtInc. DR GO; GO:0050821; P:protein stabilization; NAS:ComplexPortal. DR GO; GO:0042981; P:regulation of apoptotic process; NAS: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:0006282; P:regulation of DNA repair; ISO: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:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0000723; P:telomere maintenance; ISO:ComplexPortal. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 2.40.50.360; RuvB-like helicase, domain II; 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; IPR010339; TIP49_P-loop. DR PANTHER; PTHR11093:SF2; RUVB-LIKE 2; 1. DR PANTHER; PTHR11093; RUVB-RELATED REPTIN AND PONTIN; 1. DR Pfam; PF06068; TIP49; 1. DR Pfam; PF17856; TIP49_C; 1. DR PRINTS; PR01874; DNAREPAIRADA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR Genevisible; Q9Y230; HS. 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 //