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RuvB-like 2 (EC 3.6.4.12) (48 kDa TATA box-binding protein-interacting protein) (48 kDa TBP-interacting protein) (51 kDa erythrocyte cytosolic protein) (ECP-51) (INO80 complex subunit J) (Repressing pontin 52) (Reptin 52) (TIP49b) (TIP60-associated protein 54-beta) (TAP54-beta)

 RUVB2_HUMAN             Reviewed;         463 AA.
Q9Y230; B3KQ59; E7ETE5; Q6FIB9; Q6PK27; Q9Y361;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 199.
RecName: Full=RuvB-like 2;
EC=3.6.4.12;
AltName: Full=48 kDa TATA box-binding protein-interacting protein;
Short=48 kDa TBP-interacting protein;
AltName: Full=51 kDa erythrocyte cytosolic protein;
Short=ECP-51;
AltName: Full=INO80 complex subunit J;
AltName: Full=Repressing pontin 52;
Short=Reptin 52;
AltName: Full=TIP49b;
AltName: Full=TIP60-associated protein 54-beta;
Short=TAP54-beta;
Name=RUVBL2; Synonyms=INO80J, TIP48, TIP49B; ORFNames=CGI-46;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 72-83;
131-144; 212-223; 369-372 AND 440-457.
TISSUE=Bone marrow;
PubMed=10524211; DOI=10.1016/S0167-4781(99)00104-9;
Salzer U., Kubicek M., Prohaska R.;
"Isolation, molecular characterization, and tissue-specific expression
of ECP-51 and ECP-54 (TIP49), two homologous, interacting erythroid
cytosolic proteins.";
Biochim. Biophys. Acta 1446:365-370(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, AND
INTERACTION WITH RUVBL1.
TISSUE=Liver;
PubMed=10428817; DOI=10.1074/jbc.274.32.22437;
Kanemaki M., Kurokawa Y., Matsu-ura T., Makino Y., Masani A.,
Okazaki K., Morishita T., Tamura T.-A.;
"TIP49b, a new RuvB-like DNA helicase, is included in a complex
together with another RuvB-like DNA helicase, TIP49a.";
J. Biol. Chem. 274:22437-22444(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Mammary gland;
PubMed=10998447; DOI=10.1016/S0003-3995(00)01016-9;
Parfait B., Giovangrandi Y., Asheuer M., Laurendeau I., Olivi M.,
Vodovar N., Vidaud D., Vidaud M., Bieche I.;
"Human TIP49b/RUVBL2 gene: genomic structure, expression pattern,
physical link to the human CGB/LHB gene cluster on chromosome
19q13.3.";
Ann. Genet. 43:69-74(2000).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal liver;
PubMed=11080158; DOI=10.1093/emboj/19.22.6121;
Bauer A., Chauvet S., Huber O., Usseglio F., Rothbaecher U.,
Aragnol D., Kemler R., Pradel J.;
"Pontin52 and reptin52 function as antagonistic regulators of beta-
catenin signalling activity.";
EMBO J. 19:6121-6130(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 73-83;
116-124; 237-253 AND 254-269, AND INTERACTION WITH MYC.
PubMed=10882073; DOI=10.1016/S1097-2765(00)80427-X;
Wood M.A., McMahon S.B., Cole M.D.;
"An ATPase/helicase complex is an essential cofactor for oncogenic
transformation by c-Myc.";
Mol. Cell 5:321-330(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=10810093; DOI=10.1101/gr.10.5.703;
Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
"Identification of novel human genes evolutionarily conserved in
Caenorhabditis elegans by comparative proteomics.";
Genome Res. 10:703-713(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Embryo, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[13]
PROTEIN SEQUENCE OF 2-14.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[14]
PROTEIN SEQUENCE OF 2-18; 30-53; 55-64; 72-83; 116-124; 165-177;
237-269; 335-368; 393-400 AND 418-438, CLEAVAGE OF INITIATOR
METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 30-40; 185-197; 354-365 AND 417-427,
IDENTIFICATION IN THE NUA4 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=10966108; DOI=10.1016/S0092-8674(00)00051-9;
Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J.,
Horikoshi M., Scully R., Qin J., Nakatani Y.;
"Involvement of the TIP60 histone acetylase complex in DNA repair and
apoptosis.";
Cell 102:463-473(2000).
[16]
PROTEIN SEQUENCE OF 30-40; 72-83; 165-177; 187-197; 254-269; 354-365;
418-438 AND 445-463, IDENTIFICATION IN NUA4 COMPLEX, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=12963728; DOI=10.1074/jbc.C300389200;
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
Conaway R.C., Conaway J.W.;
"Identification of new subunits of the multiprotein mammalian
TRRAP/TIP60-containing histone acetyltransferase complex.";
J. Biol. Chem. 278:42733-42736(2003).
[17]
INTERACTION WITH ATF2.
PubMed=11713276; DOI=10.1128/MCB.21.24.8398-8413.2001;
Cho S.-G., Bhoumik A., Broday L., Ivanov V., Rosenstein B., Ronai Z.;
"TIP49b, a regulator of activating transcription factor 2 response to
stress and DNA damage.";
Mol. Cell. Biol. 21:8398-8413(2001).
[18]
FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING
COMPLEX.
PubMed=14966270; DOI=10.1128/MCB.24.5.1884-1896.2004;
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
"Structural and functional conservation of the NuA4 histone
acetyltransferase complex from yeast to humans.";
Mol. Cell. Biol. 24:1884-1896(2004).
[19]
IDENTIFICATION IN THE MLL1/MLL COMPLEX.
PubMed=15960975; DOI=10.1016/j.cell.2005.04.031;
Dou Y., Milne T.A., Tackett A.J., Smith E.R., Fukuda A., Wysocka J.,
Allis C.D., Chait B.T., Hess J.L., Roeder R.G.;
"Physical association and coordinate function of the H3 K4
methyltransferase MLL1 and the H4 K16 acetyltransferase MOF.";
Cell 121:873-885(2005).
[20]
IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=16230350; DOI=10.1074/jbc.M509128200;
Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A.,
Washburn M.P., Conaway R.C., Conaway J.W.;
"A mammalian chromatin remodeling complex with similarities to the
yeast INO80 complex.";
J. Biol. Chem. 280:41207-41212(2005).
[21]
INTERACTION WITH HINT1, AND FUNCTION.
PubMed=16014379; DOI=10.1242/jcs.02437;
Weiske J., Huber O.;
"The histidine triad protein Hint1 interacts with Pontin and Reptin
and inhibits TCF-beta-catenin-mediated transcription.";
J. Cell Sci. 118:3117-3129(2005).
[22]
SUBUNIT, MUTAGENESIS OF ASP-299, AND ELECTRON MICROSCOPY OF THE
RUVBL1-RUVBL2 HETEROMER.
PubMed=17157868; DOI=10.1016/j.jmb.2006.11.030;
Puri T., Wendler P., Sigala B., Saibil H., Tsaneva I.R.;
"Dodecameric structure and ATPase activity of the human TIP48/TIP49
complex.";
J. Mol. Biol. 366:179-192(2007).
[23]
IDENTIFICATION IN THE INO80 COMPLEX, AND PROTEIN INTERACTION.
PubMed=18026119; DOI=10.1038/nsmb1332;
Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
Wang W., Nickoloff J.A., Wu C., Shi Y.;
"A YY1-INO80 complex regulates genomic stability through homologous
recombination-based repair.";
Nat. Struct. Mol. Biol. 14:1165-1172(2007).
[24]
IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH NPAT.
PubMed=17967892; DOI=10.1128/MCB.00607-07;
DeRan M., Pulvino M., Greene E., Su C., Zhao J.;
"Transcriptional activation of histone genes requires NPAT-dependent
recruitment of TRRAP-Tip60 complex to histone promoters during the
G1/S phase transition.";
Mol. Cell. Biol. 28:435-447(2008).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
INTERACTION WITH IGHMBP2.
PubMed=19299493; DOI=10.1093/hmg/ddp134;
de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
Mourelatos Z.;
"Biochemical and genetic evidence for a role of IGHMBP2 in the
translational machinery.";
Hum. Mol. Genet. 18:2115-2126(2009).
[27]
INTERACTION WITH TELO2.
PubMed=20801936; DOI=10.1101/gad.1956410;
Takai H., Xie Y., de Lange T., Pavletich N.P.;
"Tel2 structure and function in the Hsp90-dependent maturation of mTOR
and ATR complexes.";
Genes Dev. 24:2019-2030(2010).
[28]
IDENTIFICATION IN THE R2TP COMPLEX.
PubMed=20864032; DOI=10.1016/j.molcel.2010.08.037;
Horejsi Z., Takai H., Adelman C.A., Collis S.J., Flynn H., Maslen S.,
Skehel J.M., de Lange T., Boulton S.J.;
"CK2 phospho-dependent binding of R2TP complex to TEL2 is essential
for mTOR and SMG1 stability.";
Mol. Cell 39:839-850(2010).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
IDENTIFICATION IN THE INO80 COMPLEX.
PubMed=21303910; DOI=10.1074/jbc.M111.222505;
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
Conaway J.W., Conaway R.C.;
"Subunit organization of the human INO80 chromatin remodeling complex:
An evolutionarily conserved core complex catalyzes ATP-dependent
nucleosome remodeling.";
J. Biol. Chem. 286:11283-11289(2011).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-437, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
INTERACTION WITH ITFG1.
PubMed=25437307; DOI=10.7554/eLife.04449;
Kato M., Chou T.F., Yu C.Z., DeModena J., Sternberg P.W.;
"LINKIN, a new transmembrane protein necessary for cell adhesion.";
Elife 3:E04449-E04449(2014).
[34]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
FUNCTION, AND IDENTIFICATION IN THE SWR1-LIKE COMPLEX.
PubMed=24463511; DOI=10.1038/nature12922;
Obri A., Ouararhni K., Papin C., Diebold M.L., Padmanabhan K.,
Marek M., Stoll I., Roy L., Reilly P.T., Mak T.W., Dimitrov S.,
Romier C., Hamiche A.;
"ANP32E is a histone chaperone that removes H2A.Z from chromatin.";
Nature 505:648-653(2014).
[36]
FUNCTION.
PubMed=25652260; DOI=10.15252/embr.201439123;
Marza E., Taouji S., Barroso K., Raymond A.A., Guignard L., Bonneu M.,
Pallares-Lupon N., Dupuy J.W., Fernandez-Zapico M.E., Rosenbaum J.,
Palladino F., Dupuy D., Chevet E.;
"Genome-wide screen identifies a novel p97/CDC-48-dependent pathway
regulating ER-stress-induced gene transcription.";
EMBO Rep. 16:332-340(2015).
[37]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[38]
INTERACTION WITH WAC.
PubMed=26812014; DOI=10.1016/j.devcel.2015.12.019;
David-Morrison G., Xu Z., Rui Y.N., Charng W.L., Jaiswal M.,
Yamamoto S., Xiong B., Zhang K., Sandoval H., Duraine L., Zuo Z.,
Zhang S., Bellen H.J.;
"WAC regulates mTOR activity by acting as an adaptor for the TTT and
Pontin/Reptin complexes.";
Dev. Cell 36:139-151(2016).
[39]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-9; LYS-444 AND LYS-456, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[40]
STRUCTURE BY NMR OF 132-213.
Mycobacterium tuberculosis structural genomics consortium (TB);
"Solution structure of RSGI RUH-039, a fragment of C-terminal domain
of RuvB-like 2 from human cDNA.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
dependent DNA helicase (5' to 3') activity; hexamerization is
thought to be critical for ATP hydrolysis and adjacent subunits in
the ring-like structure contribute to the ATPase activity.
-!- FUNCTION: Component of the NuA4 histone acetyltransferase complex
which is involved in transcriptional activation of select genes
principally by acetylation of nucleosomal histones H4 and H2A.
This modification may both alter nucleosome - DNA interactions and
promote interaction of the modified histones with other proteins
which positively regulate transcription. This complex may be
required for the activation of transcriptional programs associated
with oncogene and proto-oncogene mediated growth induction, tumor
suppressor mediated growth arrest and replicative senescence,
apoptosis, and DNA repair. The NuA4 complex ATPase and helicase
activities seem to be, at least in part, contributed by the
association of RUVBL1 and RUVBL2 with EP400. NuA4 may also play a
direct role in DNA repair when recruited to sites of DNA damage.
Component of a SWR1-like complex that specifically mediates the
removal of histone H2A.Z/H2AFZ from the nucleosome.
-!- FUNCTION: Proposed core component of the chromatin remodeling
INO80 complex which is involved in transcriptional regulation, DNA
replication and probably DNA repair.
-!- FUNCTION: Plays an essential role in oncogenic transformation by
MYC and also modulates transcriptional activation by the
LEF1/TCF1-CTNNB1 complex. May also inhibit the transcriptional
activity of ATF2.
-!- FUNCTION: Involved in the endoplasmic reticulum (ER)-associated
degradation (ERAD) pathway where it negatively regulates
expression of ER stress response genes.
{ECO:0000269|PubMed:25652260}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Forms homohexameric rings (Probable). Can form a
dodecamer with RUVBL1 made of two stacked hexameric rings;
however, even though RUVBL1 and RUVBL2 are present in equimolar
ratio, the oligomeric status of each hexamer is not known.
Oligomerization may regulate binding to nucleic acids and
conversely, binding to nucleic acids may affect the dodecameric
assembly. Interacts with the transcriptional activation domain of
MYC. Interacts With ATF2. Component of the RNA polymerase II
holoenzyme complex. May also act to bridge the LEF1/TCF1-CTNNB1
complex and TBP. Component of the NuA4 histone acetyltransferase
complex which contains the catalytic subunit KAT5/TIP60 and the
subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15,
MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4
complex interacts with MYC and the adenovirus E1A protein. RUVBL2
interacts with EP400. Component of a NuA4-related complex which
contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1,
DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72
and YEATS4/GAS41. Interacts with NPAT. Component of the chromatin-
remodeling INO80 complex; specifically part of a complex module
associated with the helicase ATP-binding and the helicase C-
terminal domain of INO80. Component of some MLL1/MLL complex, at
least composed of the core components KMT2A/MLL1, ASH2L,
HCFC1/HCF1, WDR5 and RBBP5, as well as the facultative components
BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1, LAS1L, MAX, MCRS1, MGA,
MYST1/MOF, PELP1, PHF20, PRP31, RING2, RUVB1/TIP49A, RUVB2/TIP49B,
SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and TEX10. Interacts with
IGHMBP2. Interacts with TELO2. Interacts with HINT1. Component of
a SWR1-like complex. Component of the R2TP complex composed at
least of PIHD1, RUVBL1, RUVBL2 and RPAP3 (PubMed:20864032).
Interacts with ITFG1 (PubMed:25437307). Interacts with WAC; WAC
positively regulates MTOR activity by promoting the assembly of
the TTT complex composed of TELO2, TTI1 and TTI2 and the RUVBL
complex composed of RUVBL1 and RUVBL2 into the TTT-RUVBL complex
which leads to the dimerization of the mTORC1 complex and its
subsequent activation (PubMed:26812014).
{ECO:0000269|PubMed:10428817, ECO:0000269|PubMed:10882073,
ECO:0000269|PubMed:10966108, ECO:0000269|PubMed:11713276,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270,
ECO:0000269|PubMed:15960975, ECO:0000269|PubMed:16014379,
ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:17157868,
ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:18026119,
ECO:0000269|PubMed:19299493, ECO:0000269|PubMed:20801936,
ECO:0000269|PubMed:20864032, ECO:0000269|PubMed:21303910,
ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:25437307,
ECO:0000269|PubMed:26812014, ECO:0000305}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-352939, EBI-352939;
Q8IW40:CCDC103; NbExp=3; IntAct=EBI-352939, EBI-10261970;
Q9BVM2:DPCD; NbExp=6; IntAct=EBI-352939, EBI-749988;
Q8TBB1:LNX1; NbExp=5; IntAct=EBI-352939, EBI-739832;
Q9Y265:RUVBL1; NbExp=26; IntAct=EBI-352939, EBI-353675;
P25490:YY1; NbExp=6; IntAct=EBI-352939, EBI-765538;
-!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
Cytoplasm. Membrane. Note=Mainly localized in the nucleus,
associated with nuclear matrix or in the nuclear cytosol. Although
it is also present in the cytoplasm and associated with the cell
membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y230-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y230-2; Sequence=VSP_056584;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
testis and thymus.
-!- DOMAIN: The C-terminal domain is required for association with
ATF2.
-!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD34041.1; Type=Frameshift; Positions=401; Evidence={ECO:0000305};
Sequence=AAH08355.1; Type=Frameshift; Positions=191; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RUVBL2ID42185ch19q13.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; Y18417; CAB46270.1; -; mRNA.
EMBL; AB024301; BAA76708.1; -; mRNA.
EMBL; AF155138; AAD38073.1; -; mRNA.
EMBL; AF124607; AAF87087.1; -; mRNA.
EMBL; AF151804; AAD34041.1; ALT_FRAME; mRNA.
EMBL; AL136743; CAB66677.1; -; mRNA.
EMBL; AK057498; BAG51921.1; -; mRNA.
EMBL; AK074542; BAC11048.1; -; mRNA.
EMBL; CR533507; CAG38538.1; -; mRNA.
EMBL; AC008687; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471177; EAW52426.1; -; Genomic_DNA.
EMBL; CH471177; EAW52430.1; -; Genomic_DNA.
EMBL; BC000428; AAH00428.1; -; mRNA.
EMBL; BC004531; AAH04531.1; -; mRNA.
EMBL; BC008355; AAH08355.1; ALT_FRAME; mRNA.
CCDS; CCDS42588.1; -. [Q9Y230-1]
PIR; T46313; T46313.
RefSeq; NP_001308120.1; NM_001321191.1. [Q9Y230-2]
RefSeq; NP_006657.1; NM_006666.2. [Q9Y230-1]
RefSeq; XP_011524632.1; XM_011526330.1. [Q9Y230-2]
UniGene; Hs.515846; -.
PDB; 2CQA; NMR; -; A=132-213.
PDB; 2XSZ; X-ray; 3.00 A; D/E/F=2-133, D/E/F=238-463.
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.
PDBsum; 2CQA; -.
PDBsum; 2XSZ; -.
PDBsum; 3UK6; -.
ProteinModelPortal; Q9Y230; -.
SMR; Q9Y230; -.
BioGrid; 116067; 249.
DIP; DIP-28153N; -.
IntAct; Q9Y230; 114.
MINT; MINT-1136527; -.
STRING; 9606.ENSP00000473172; -.
ChEMBL; CHEMBL2062349; -.
iPTMnet; Q9Y230; -.
PhosphoSitePlus; Q9Y230; -.
SwissPalm; Q9Y230; -.
BioMuta; RUVBL2; -.
DMDM; 28201890; -.
REPRODUCTION-2DPAGE; IPI00009104; -.
EPD; Q9Y230; -.
PaxDb; Q9Y230; -.
PeptideAtlas; Q9Y230; -.
PRIDE; Q9Y230; -.
DNASU; 10856; -.
Ensembl; ENST00000595090; ENSP00000473172; ENSG00000183207. [Q9Y230-1]
GeneID; 10856; -.
KEGG; hsa:10856; -.
UCSC; uc002plr.2; human. [Q9Y230-1]
CTD; 10856; -.
DisGeNET; 10856; -.
GeneCards; RUVBL2; -.
HGNC; HGNC:10475; RUVBL2.
HPA; CAB012432; -.
HPA; HPA042880; -.
HPA; HPA067966; -.
MIM; 604788; gene.
neXtProt; NX_Q9Y230; -.
OpenTargets; ENSG00000183207; -.
PharmGKB; PA34888; -.
eggNOG; KOG2680; Eukaryota.
eggNOG; COG1224; LUCA.
GeneTree; ENSGT00890000139527; -.
HOGENOM; HOG000190885; -.
HOVERGEN; HBG054186; -.
InParanoid; Q9Y230; -.
KO; K11338; -.
OMA; VPFTMIA; -.
OrthoDB; EOG091G07C9; -.
PhylomeDB; Q9Y230; -.
TreeFam; TF300469; -.
Reactome; R-HSA-171319; Telomere Extension By Telomerase.
Reactome; R-HSA-3214847; HATs acetylate histones.
ChiTaRS; RUVBL2; human.
EvolutionaryTrace; Q9Y230; -.
GeneWiki; RUVBL2; -.
GenomeRNAi; 10856; -.
PRO; PR:Q9Y230; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000183207; -.
CleanEx; HS_RUVBL2; -.
ExpressionAtlas; Q9Y230; baseline and differential.
Genevisible; Q9Y230; HS.
GO; GO:0005813; C:centrosome; IDA:HPA.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0097255; C:R2TP complex; IDA:UniProtKB.
GO; GO:0000812; C:Swr1 complex; IDA:UniProtKB.
GO; GO:0043531; F:ADP binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IEA:InterPro.
GO; GO:0004003; F:ATP-dependent DNA helicase activity; TAS:ProtInc.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0000980; F:RNA polymerase II distal enhancer sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001094; F:TFIID-class transcription factor binding; IEA:Ensembl.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
GO; GO:0071392; P:cellular response to estradiol stimulus; IMP:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IMP:UniProtKB.
GO; GO:0006310; P:DNA recombination; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; TAS:ProtInc.
GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0071899; P:negative regulation of estrogen receptor binding; IMP:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:UniProtKB.
GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:UniProtKB.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0071733; P:transcriptional activation by promoter-enhancer looping; IMP:UniProtKB.
InterPro; IPR003593; AAA+_ATPase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR027238; RuvB-like.
InterPro; IPR010339; TIP49_C.
PANTHER; PTHR11093; PTHR11093; 1.
Pfam; PF06068; TIP49; 1.
SMART; SM00382; AAA; 1.
SUPFAM; SSF52540; SSF52540; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Chromatin regulator; Complete proteome; Cytoplasm;
Direct protein sequencing; DNA damage; DNA recombination; DNA repair;
Growth regulation; Helicase; Hydrolase; Isopeptide bond; Membrane;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|Ref.14}.
CHAIN 2 463 RuvB-like 2.
/FTId=PRO_0000165644.
NP_BIND 77 84 ATP.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.14}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 9 9 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 456 456 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 45 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056584.
MUTAGEN 299 299 D->N: Abolishes ATPase activity.
{ECO:0000269|PubMed:17157868}.
CONFLICT 214 214 D -> N (in Ref. 6; AAD34041).
{ECO:0000305}.
CONFLICT 257 258 FL -> YV (in Ref. 5; AA sequence).
{ECO:0000305}.
TURN 19 22 {ECO:0000244|PDB:3UK6}.
TURN 24 27 {ECO:0000244|PDB:2XSZ}.
STRAND 41 43 {ECO:0000244|PDB:3UK6}.
STRAND 46 48 {ECO:0000244|PDB:3UK6}.
HELIX 50 64 {ECO:0000244|PDB:3UK6}.
STRAND 72 78 {ECO:0000244|PDB:3UK6}.
HELIX 83 94 {ECO:0000244|PDB:3UK6}.
STRAND 100 104 {ECO:0000244|PDB:3UK6}.
HELIX 105 108 {ECO:0000244|PDB:3UK6}.
STRAND 111 113 {ECO:0000244|PDB:3UK6}.
HELIX 115 125 {ECO:0000244|PDB:3UK6}.
STRAND 126 129 {ECO:0000244|PDB:3UK6}.
STRAND 136 148 {ECO:0000244|PDB:2CQA}.
STRAND 152 156 {ECO:0000244|PDB:2CQA}.
STRAND 158 164 {ECO:0000244|PDB:2CQA}.
STRAND 166 174 {ECO:0000244|PDB:2CQA}.
HELIX 177 184 {ECO:0000244|PDB:2CQA}.
STRAND 191 196 {ECO:0000244|PDB:2CQA}.
TURN 197 200 {ECO:0000244|PDB:2CQA}.
STRAND 201 206 {ECO:0000244|PDB:2CQA}.
HELIX 241 247 {ECO:0000244|PDB:3UK6}.
HELIX 267 283 {ECO:0000244|PDB:3UK6}.
STRAND 292 297 {ECO:0000244|PDB:3UK6}.
HELIX 298 300 {ECO:0000244|PDB:3UK6}.
HELIX 303 312 {ECO:0000244|PDB:3UK6}.
STRAND 320 326 {ECO:0000244|PDB:3UK6}.
STRAND 328 331 {ECO:0000244|PDB:3UK6}.
STRAND 332 334 {ECO:0000244|PDB:2XSZ}.
STRAND 338 340 {ECO:0000244|PDB:3UK6}.
STRAND 341 343 {ECO:0000244|PDB:2XSZ}.
HELIX 345 348 {ECO:0000244|PDB:3UK6}.
STRAND 351 356 {ECO:0000244|PDB:3UK6}.
HELIX 361 374 {ECO:0000244|PDB:3UK6}.
HELIX 381 393 {ECO:0000244|PDB:3UK6}.
HELIX 396 412 {ECO:0000244|PDB:3UK6}.
STRAND 416 418 {ECO:0000244|PDB:3UK6}.
HELIX 420 429 {ECO:0000244|PDB:3UK6}.
HELIX 433 440 {ECO:0000244|PDB:3UK6}.
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


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Genprice Inc, Invoices and accounting
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