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RuvB-like 1 (EC 3.6.4.12) (49 kDa TATA box-binding protein-interacting protein) (49 kDa TBP-interacting protein) (54 kDa erythrocyte cytosolic protein) (ECP-54) (INO80 complex subunit H) (Nuclear matrix protein 238) (NMP 238) (Pontin 52) (TIP49a) (TIP60-associated protein 54-alpha) (TAP54-alpha)

 RUVB1_HUMAN             Reviewed;         456 AA.
Q9Y265; B2R5S0; P82276; Q1KMR0; Q53HK5; Q53HL7; Q53Y27; Q9BSX9;
01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
30-AUG-2017, entry version 186.
RecName: Full=RuvB-like 1;
EC=3.6.4.12;
AltName: Full=49 kDa TATA box-binding protein-interacting protein;
Short=49 kDa TBP-interacting protein;
AltName: Full=54 kDa erythrocyte cytosolic protein;
Short=ECP-54;
AltName: Full=INO80 complex subunit H;
AltName: Full=Nuclear matrix protein 238;
Short=NMP 238;
AltName: Full=Pontin 52;
AltName: Full=TIP49a;
AltName: Full=TIP60-associated protein 54-alpha;
Short=TAP54-alpha;
Name=RUVBL1; Synonyms=INO80H, NMP238, TIP49, TIP49A;
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).
TISSUE=Liver;
PubMed=9588198; DOI=10.1006/bbrc.1998.8504;
Makino Y., Mimori T., Koike C., Kanemaki M., Kurokawa Y., Inoue S.,
Kishimoto T., Tamura T.-A.;
"TIP49, homologous to the bacterial DNA helicase RuvB, acts as an
autoantigen in human.";
Biochem. Biophys. Res. Commun. 245:819-823(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 1-7.
TISSUE=Pancreas;
PubMed=9813143; DOI=10.1006/bbrc.1998.9604;
Holzmann K., Gerner C., Korosec T., Poeltl A., Grimm R., Sauermann G.;
"Identification and characterization of the ubiquitously occurring
nuclear matrix protein NMP 238.";
Biochem. Biophys. Res. Commun. 252:39-45(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=9774387; DOI=10.1074/jbc.273.43.27786;
Qiu X.-B., Lin Y.-L., Thome K.C., Pian P., Schlegel B.P.,
Weremowicz S., Parvin J.D., Dutta A.;
"An eukaryotic RuvB-like protein (RUVBL1) essential for growth.";
J. Biol. Chem. 273:27786-27793(1998).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Colon adenocarcinoma;
PubMed=9843967; DOI=10.1073/pnas.95.25.14787;
Bauer A., Huber O., Kemler R.;
"Pontin52, an interaction partner of beta-catenin, binds to the TATA
box binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 95:14787-14792(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEIN SEQUENCE OF 34-46;
108-118; 169-177; 207-219 AND 446-456.
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 172-182
AND 184-201, AND FUNCTION.
PubMed=11027681; DOI=10.1074/jbc.M004919200;
Hawley S.B., Tamura T.-A., Miles L.A.;
"Purification, cloning, and characterization of a profibrinolytic
plasminogen-binding protein, TIP49a.";
J. Biol. Chem. 276:179-186(2001).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
Huber O., Orso S.;
"The genomic structure of the human pontin 52 gene.";
Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Koc F., Gartner W., Birkenkamp-Demtroeder K., Altenberger T.,
Daneva T., Wagner L.;
"RUVBL1-FK- splice variant.";
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Cerebellum;
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Adipose tissue, and Coronary artery;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=19054851; DOI=10.1038/nmeth.1273;
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
Isogai T., Imai J., Watanabe S., Nomura N.;
"Human protein factory for converting the transcriptome into an in
vitro-expressed proteome.";
Nat. Methods 5:1011-1017(2008).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=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).
[14]
PROTEIN SEQUENCE OF 23-33; 65-90; 153-162; 172-182; 318-333; 340-357;
363-372 AND 379-400, AND IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[15]
PROTEIN SEQUENCE OF 23-33 AND 77-90, INTERACTION WITH MYC, AND
MUTAGENESIS OF ASP-302.
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).
[16]
PROTEIN SEQUENCE OF 23-33; 34-46; 77-90; 172-182; 185-201; 340-357 AND
405-418 (ISOFORM 1), 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]
PROTEIN SEQUENCE OF 34-46 AND 108-117, IDENTIFICATION IN 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).
[18]
PROTEIN SEQUENCE OF 34-46, FUNCTION, INTERACTION WITH TUBULIN, AND
SUBCELLULAR LOCATION.
TISSUE=Monocyte;
PubMed=14506706; DOI=10.1002/cm.10136;
Gartner W., Rossbacher J., Zierhut B., Daneva T., Base W., Weissel M.,
Waldhausl W., Pasternack M.S., Wagner L.;
"The ATP-dependent helicase RUVBL1/TIP49a associates with tubulin
during mitosis.";
Cell Motil. Cytoskeleton 56:79-93(2003).
[19]
INTERACTION WITH RUVBL2.
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).
[20]
FUNCTION.
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).
[21]
IDENTIFICATION IN BAF53 COMPLEX WITH ACTL6A; SMARCA2 AND TRRAP.
PubMed=11839798; DOI=10.1128/MCB.22.5.1307-1316.2002;
Park J., Wood M.A., Cole M.D.;
"BAF53 forms distinct nuclear complexes and functions as a critical c-
Myc-interacting nuclear cofactor for oncogenic transformation.";
Mol. Cell. Biol. 22:1307-1316(2002).
[22]
FUNCTION, AND MUTAGENESIS OF ASP-302.
PubMed=14695187;
Feng Y., Lee N., Fearon E.R.;
"TIP49 regulates beta-catenin-mediated neoplastic transformation and
T-cell factor target gene induction via effects on chromatin
remodeling.";
Cancer Res. 63:8726-8734(2003).
[23]
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).
[24]
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).
[25]
IDENTIFICATION IN THE 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).
[26]
INTERACTION WITH HINT1, FUNCTION, AND SUBCELLULAR LOCATION.
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).
[27]
SUBUNIT, MUTAGENESIS OF ASP-302, 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).
[28]
INTERACTION WITH OFD1.
PubMed=17761535; DOI=10.1091/mbc.E07-03-0198;
Giorgio G., Alfieri M., Prattichizzo C., Zullo A., Cairo S.,
Franco B.;
"Functional characterization of the OFD1 protein reveals a nuclear
localization and physical interaction with subunits of a chromatin
remodeling complex.";
Mol. Biol. Cell 18:4397-4404(2007).
[29]
INTERACTION WITH PIH1D1.
PubMed=17636026; DOI=10.1128/MCB.01097-07;
McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.;
"A dynamic scaffold of pre-snoRNP factors facilitates human box C/D
snoRNP assembly.";
Mol. Cell. Biol. 27:6782-6793(2007).
[30]
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).
[31]
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).
[32]
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).
[33]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-453, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[34]
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).
[35]
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).
[36]
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).
[37]
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).
[38]
IDENTIFICATION IN A COMPLEX WITH USP49 AND PSMC5.
PubMed=23824326; DOI=10.1101/gad.211037.112;
Zhang Z., Jones A., Joo H.Y., Zhou D., Cao Y., Chen S.,
Erdjument-Bromage H., Renfrow M., He H., Tempst P., Townes T.M.,
Giles K.E., Ma L., Wang H.;
"USP49 deubiquitinates histone H2B and regulates cotranscriptional
pre-mRNA splicing.";
Genes Dev. 27:1581-1595(2013).
[39]
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).
[40]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[41]
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).
[42]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-225, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[43]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[44]
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).
[45]
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).
[46]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-2; LYS-225 AND LYS-445, 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).
[47]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF
ASP-302.
PubMed=17060327; DOI=10.1074/jbc.M605625200;
Matias P.M., Gorynia S., Donner P., Carrondo M.A.;
"Crystal structure of the human AAA+ protein RuvBL1.";
J. Biol. Chem. 281:38918-38929(2006).
-!- FUNCTION: Possesses single-stranded DNA-stimulated ATPase and ATP-
dependent DNA helicase (3' to 5') 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. Essential for cell proliferation.
-!- FUNCTION: May be able to bind plasminogen at cell surface and
enhance plasminogen activation.
-!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
-!- SUBUNIT: Forms homohexameric rings. Can form a dodecamer with
RUVBL2 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. 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. RUVBL1 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. Component of the BAF53 complex, at least
composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM, and
TRRAP/PAF400. 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. Associates with alpha and
gamma tubulins, particularly during metaphase and early anaphase.
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.
Interacts with IGHMBP2. Interacts with OFD1. Interacts with HINT1.
Component of a complex with USP49 and PSMC5. Component of a SWR1-
like complex. Component of the R2TP complex composed at least of
PIHD1, RUVBL1, RUVBL2 and RPAP3 (PubMed:20864032). Interacts with
PIH1D1 (PubMed:17636026). 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:11839798,
ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14506706,
ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:15960975,
ECO:0000269|PubMed:16014379, ECO:0000269|PubMed:16230350,
ECO:0000269|PubMed:17060327, ECO:0000269|PubMed:17157868,
ECO:0000269|PubMed:17636026, ECO:0000269|PubMed:17761535,
ECO:0000269|PubMed:17967892, ECO:0000269|PubMed:18026119,
ECO:0000269|PubMed:19299493, ECO:0000269|PubMed:20864032,
ECO:0000269|PubMed:21303910, ECO:0000269|PubMed:23824326,
ECO:0000269|PubMed:24463511, ECO:0000269|PubMed:25437307,
ECO:0000269|PubMed:26812014}.
-!- INTERACTION:
O60832:DKC1; NbExp=8; IntAct=EBI-353675, EBI-713091;
O95905:ECD; NbExp=7; IntAct=EBI-353675, EBI-2557598;
G3I183:I79_017133 (xeno); NbExp=2; IntAct=EBI-353675, EBI-10890180;
O75665:OFD1; NbExp=3; IntAct=EBI-353675, EBI-716327;
Q9Y230:RUVBL2; NbExp=26; IntAct=EBI-353675, EBI-352939;
O14746:TERT; NbExp=11; IntAct=EBI-353675, EBI-1772203;
Q15906:VPS72; NbExp=6; IntAct=EBI-353675, EBI-399189;
P25490:YY1; NbExp=5; IntAct=EBI-353675, EBI-765538;
Q9UHR6:ZNHIT2; NbExp=4; IntAct=EBI-353675, EBI-2557592;
-!- SUBCELLULAR LOCATION: Nucleus matrix. Nucleus, nucleoplasm.
Cytoplasm. Membrane. Cytoplasm, cytoskeleton, microtubule
organizing center, centrosome. 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. In prophase and prometaphase it is located at
the centrosome and the branching microtubule spindles. After
mitotic nuclear membrane disintigration it accumulates at the
centrosome and sites of tubulin polymerization. As cells pass
through metaphase and into telophase it is located close to the
centrosome at the early phase of tubulin polymerization. In
anaphase it accumulates at the zone of tubule interdigitation. In
telophase it is found at polar tubule overlap, and it reappears at
the site of chromosomal decondensation in the daughter cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9Y265-1; Sequence=Displayed;
Name=2;
IsoId=Q9Y265-2; Sequence=VSP_021387, VSP_021388;
-!- TISSUE SPECIFICITY: Ubiquitously expressed with high expression in
heart, skeletal muscle and testis.
-!- DOMAIN: Binding to MYC is dependent on a Myc domain essential for
oncogenic activity.
-!- MISCELLANEOUS: High level of autoantibodies against RUVBL1 are
detected in sera of patients with autoimmune diseases such as
polymyositis/dermatomyosistis and autoimmune hepatitis.
-!- SIMILARITY: Belongs to the RuvB family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/RUVBL1ID44415ch3q21.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; AB012122; BAA28169.1; -; mRNA.
EMBL; AJ010058; CAA08986.1; -; mRNA.
EMBL; AF070735; AAC77819.1; -; mRNA.
EMBL; AF099084; AAD04427.1; -; mRNA.
EMBL; Y18418; CAB46271.1; -; mRNA.
EMBL; AF380344; AAM45570.1; -; Genomic_DNA.
EMBL; AF380343; AAM45570.1; JOINED; Genomic_DNA.
EMBL; DQ469310; ABF13334.1; -; mRNA.
EMBL; BT007057; AAP35706.1; -; mRNA.
EMBL; AK222563; BAD96283.1; -; mRNA.
EMBL; AK222575; BAD96295.1; -; mRNA.
EMBL; AK312290; BAG35217.1; -; mRNA.
EMBL; AB451224; BAG70038.1; -; mRNA.
EMBL; BC002993; AAH02993.1; -; mRNA.
EMBL; BC012886; AAH12886.1; -; mRNA.
CCDS; CCDS3047.1; -. [Q9Y265-1]
PIR; JE0334; JE0334.
RefSeq; NP_001306013.1; NM_001319084.1. [Q9Y265-2]
RefSeq; NP_003698.1; NM_003707.2. [Q9Y265-1]
UniGene; Hs.272822; -.
UniGene; Hs.710868; -.
PDB; 2C9O; X-ray; 2.20 A; A/B/C=1-456.
PDB; 2XSZ; X-ray; 3.00 A; A/B/C=2-126, A/B/C=234-456.
PDBsum; 2C9O; -.
PDBsum; 2XSZ; -.
ProteinModelPortal; Q9Y265; -.
SMR; Q9Y265; -.
BioGrid; 114166; 226.
DIP; DIP-29937N; -.
IntAct; Q9Y265; 95.
MINT; MINT-1138777; -.
STRING; 9606.ENSP00000318297; -.
BindingDB; Q9Y265; -.
ChEMBL; CHEMBL3259467; -.
iPTMnet; Q9Y265; -.
PhosphoSitePlus; Q9Y265; -.
SwissPalm; Q9Y265; -.
BioMuta; RUVBL1; -.
DMDM; 28201891; -.
OGP; Q9Y265; -.
REPRODUCTION-2DPAGE; Q9Y265; -.
SWISS-2DPAGE; Q9Y265; -.
EPD; Q9Y265; -.
PaxDb; Q9Y265; -.
PeptideAtlas; Q9Y265; -.
PRIDE; Q9Y265; -.
DNASU; 8607; -.
Ensembl; ENST00000322623; ENSP00000318297; ENSG00000175792. [Q9Y265-1]
GeneID; 8607; -.
KEGG; hsa:8607; -.
UCSC; uc003ekh.4; human. [Q9Y265-1]
CTD; 8607; -.
DisGeNET; 8607; -.
GeneCards; RUVBL1; -.
HGNC; HGNC:10474; RUVBL1.
HPA; HPA019947; -.
HPA; HPA019948; -.
MIM; 603449; gene.
neXtProt; NX_Q9Y265; -.
OpenTargets; ENSG00000175792; -.
PharmGKB; PA34887; -.
eggNOG; KOG1942; Eukaryota.
eggNOG; COG1224; LUCA.
GeneTree; ENSGT00890000139499; -.
HOVERGEN; HBG054186; -.
InParanoid; Q9Y265; -.
KO; K04499; -.
OMA; DVHKRKE; -.
OrthoDB; EOG091G07C9; -.
PhylomeDB; Q9Y265; -.
TreeFam; TF300457; -.
Reactome; R-HSA-171319; Telomere Extension By Telomerase.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3214847; HATs acetylate histones.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
ChiTaRS; RUVBL1; human.
EvolutionaryTrace; Q9Y265; -.
GeneWiki; RuvB-like_1; -.
GenomeRNAi; 8607; -.
PRO; PR:Q9Y265; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000175792; -.
CleanEx; HS_RUVBL1; -.
ExpressionAtlas; Q9Y265; baseline and differential.
Genevisible; Q9Y265; HS.
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:0030529; C:intracellular ribonucleoprotein complex; IEA:Ensembl.
GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
GO; GO:0071339; C:MLL1 complex; IDA:UniProtKB.
GO; GO:0035267; C:NuA4 histone acetyltransferase complex; 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; IBA:GO_Central.
GO; GO:0016887; F:ATPase activity; IDA:UniProtKB.
GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
GO; GO:0001094; F:TFIID-class transcription factor binding; IEA:Ensembl.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0000492; P:box C/D snoRNP assembly; IBA:GO_Central.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0034080; P:CENP-A containing nucleosome assembly; TAS:Reactome.
GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; IMP:ParkinsonsUK-UCL.
GO; GO:1904874; P:positive regulation of telomerase RNA localization to Cajal body; IMP:BHF-UCL.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
GO; GO:1903146; P:regulation of mitophagy; IMP:ParkinsonsUK-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
GO; GO:0007283; P:spermatogenesis; TAS:ProtInc.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Cell cycle; Cell division; Chromatin regulator;
Complete proteome; Cytoplasm; Cytoskeleton; Direct protein sequencing;
DNA damage; DNA recombination; DNA repair; Growth regulation;
Helicase; Hydrolase; Isopeptide bond; Membrane; Mitosis;
Nucleotide-binding; Nucleus; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 456 RuvB-like 1.
/FTId=PRO_0000165639.
NP_BIND 70 77 ATP. {ECO:0000250}.
MOD_RES 453 453 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
CROSSLNK 2 2 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 225 225 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 374 386 IIKIRAQTEGINI -> VLSAAADPGQLAC (in
isoform 2). {ECO:0000303|Ref.8}.
/FTId=VSP_021387.
VAR_SEQ 387 456 Missing (in isoform 2).
{ECO:0000303|Ref.8}.
/FTId=VSP_021388.
MUTAGEN 302 302 D->N: Abolishes ATPase activity;
inhibition of MYC- and CTNNB1-mediated
transformation.
{ECO:0000269|PubMed:10882073,
ECO:0000269|PubMed:14695187,
ECO:0000269|PubMed:17060327,
ECO:0000269|PubMed:17157868}.
CONFLICT 52 52 I -> T (in Ref. 12; BAD96283).
{ECO:0000305}.
CONFLICT 145 145 N -> D (in Ref. 12; BAD96295).
{ECO:0000305}.
CONFLICT 285 285 K -> R (in Ref. 8; ABF13334).
{ECO:0000305}.
CONFLICT 353 353 D -> P (in Ref. 8; ABF13334).
{ECO:0000305}.
HELIX 10 16 {ECO:0000244|PDB:2C9O}.
TURN 17 20 {ECO:0000244|PDB:2C9O}.
STRAND 28 30 {ECO:0000244|PDB:2XSZ}.
STRAND 34 36 {ECO:0000244|PDB:2C9O}.
STRAND 39 41 {ECO:0000244|PDB:2C9O}.
HELIX 43 57 {ECO:0000244|PDB:2C9O}.
STRAND 65 69 {ECO:0000244|PDB:2C9O}.
STRAND 72 75 {ECO:0000244|PDB:2XSZ}.
HELIX 76 87 {ECO:0000244|PDB:2C9O}.
STRAND 93 97 {ECO:0000244|PDB:2C9O}.
HELIX 98 101 {ECO:0000244|PDB:2C9O}.
STRAND 104 106 {ECO:0000244|PDB:2C9O}.
HELIX 108 118 {ECO:0000244|PDB:2C9O}.
STRAND 119 140 {ECO:0000244|PDB:2C9O}.
STRAND 157 163 {ECO:0000244|PDB:2C9O}.
STRAND 166 172 {ECO:0000244|PDB:2C9O}.
HELIX 174 182 {ECO:0000244|PDB:2C9O}.
STRAND 189 194 {ECO:0000244|PDB:2C9O}.
TURN 195 197 {ECO:0000244|PDB:2C9O}.
STRAND 200 206 {ECO:0000244|PDB:2C9O}.
STRAND 216 221 {ECO:0000244|PDB:2C9O}.
STRAND 228 239 {ECO:0000244|PDB:2C9O}.
HELIX 240 245 {ECO:0000244|PDB:2C9O}.
HELIX 278 288 {ECO:0000244|PDB:2C9O}.
STRAND 291 296 {ECO:0000244|PDB:2C9O}.
STRAND 298 303 {ECO:0000244|PDB:2C9O}.
HELIX 304 306 {ECO:0000244|PDB:2C9O}.
HELIX 309 318 {ECO:0000244|PDB:2C9O}.
STRAND 326 331 {ECO:0000244|PDB:2C9O}.
STRAND 334 337 {ECO:0000244|PDB:2C9O}.
STRAND 345 347 {ECO:0000244|PDB:2C9O}.
HELIX 352 355 {ECO:0000244|PDB:2C9O}.
STRAND 358 362 {ECO:0000244|PDB:2C9O}.
HELIX 368 382 {ECO:0000244|PDB:2C9O}.
HELIX 388 400 {ECO:0000244|PDB:2C9O}.
HELIX 403 408 {ECO:0000244|PDB:2C9O}.
HELIX 410 419 {ECO:0000244|PDB:2C9O}.
STRAND 423 425 {ECO:0000244|PDB:2C9O}.
HELIX 427 436 {ECO:0000244|PDB:2C9O}.
HELIX 440 448 {ECO:0000244|PDB:2C9O}.
SEQUENCE 456 AA; 50228 MW; 6095ADE692B1482B CRC64;
MKIEEVKSTT KTQRIASHSH VKGLGLDESG LAKQAASGLV GQENAREACG VIVELIKSKK
MAGRAVLLAG PPGTGKTALA LAIAQELGSK VPFCPMVGSE VYSTEIKKTE VLMENFRRAI
GLRIKETKEV YEGEVTELTP CETENPMGGY GKTISHVIIG LKTAKGTKQL KLDPSIFESL
QKERVEAGDV IYIEANSGAV KRQGRCDTYA TEFDLEAEEY VPLPKGDVHK KKEIIQDVTL
HDLDVANARP QGGQDILSMM GQLMKPKKTE ITDKLRGEIN KVVNKYIDQG IAELVPGVLF
VDEVHMLDIE CFTYLHRALE SSIAPIVIFA SNRGNCVIRG TEDITSPHGI PLDLLDRVMI
IRTMLYTPQE MKQIIKIRAQ TEGINISEEA LNHLGEIGTK TTLRYSVQLL TPANLLAKIN
GKDSIEKEHV EEISELFYDA KSSAKILADQ QDKYMK


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EIAAB29755 Mouse,Mus musculus,PABP-interacting protein 2,Paip2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB29751 PABP-interacting protein 2,Paip2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2,Rat,Rattus norvegicus
EIAAB29752 Bos taurus,Bovine,PABP-interacting protein 2,PAIP2,PAIP-2,Poly(A)-binding protein-interacting protein 2,Polyadenylate-binding protein-interacting protein 2
EIAAB42299 fSAP24,Functional spliceosome-associated protein 24,Homo sapiens,hTREX30,Human,Ngg1-interacting factor 3-like protein 1-binding protein 1,NIF3L1-binding protein 1,NIF3L1BP1,THO complex subunit 7 homol
EIAAB39603 54 kDa VacA-interacting protein,90 kDa N-WASP-interacting protein,90 kDa SH3 protein interacting with Nck,Mouse,Mus musculus,NCK-interacting protein with SH3 domain,Nckipsd,N-WASP-binding protein,SH3


 

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