DDX21_HUMAN
ID DDX21_HUMAN Reviewed; 783 AA.
AC Q9NR30; B2RDL0; Q13436; Q5VX41; Q68D35;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 5.
DT 03-AUG-2022, entry version 224.
DE RecName: Full=Nucleolar RNA helicase 2 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305};
DE AltName: Full=DEAD box protein 21;
DE AltName: Full=Gu-alpha;
DE AltName: Full=Nucleolar RNA helicase Gu;
DE AltName: Full=Nucleolar RNA helicase II;
DE AltName: Full=RH II/Gu;
GN Name=DDX21;
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), SUBCELLULAR LOCATION, AND VARIANT
RP ILE-27.
RX PubMed=8614622; DOI=10.1093/nar/24.7.1220;
RA Valdez B.C., Henning D., Busch R.K., Woods K., Flores-Rozas H., Hurwitz J.,
RA Perlaky L., Busch H.;
RT "A nucleolar RNA helicase recognized by autoimmune antibodies from a
RT patient with watermelon stomach disease.";
RL Nucleic Acids Res. 24:1220-1224(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ILE-27.
RC TISSUE=Cervix adenocarcinoma;
RX PubMed=11237763; DOI=10.1006/bbrc.2001.4446;
RA Zhu K., Henning D., Valdez B.C., Busch H.;
RT "Human RNA helicase II/Gu gene: genomic organization and promoter
RT analysis.";
RL Biochem. Biophys. Res. Commun. 281:1006-1011(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Uterine endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Muscle;
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 [8]
RP PROTEIN SEQUENCE OF 7-18; 117-131; 185-199; 205-215; 237-247; 258-270;
RP 287-304; 307-318; 364-387; 392-402; 407-417; 424-432; 450-474; 485-499;
RP 545-555; 606-627; 659-668; 679-696 AND 703-718, PHOSPHORYLATION AT SER-121,
RP AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 185-199; 260-270 AND 563-573, FUNCTION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH JUN.
RX PubMed=11823437; DOI=10.1093/emboj/21.3.451;
RA Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M.,
RA Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.;
RT "The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated
RT transcription.";
RL EMBO J. 21:451-460(2002).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, AND MUTAGENESIS OF 339-ASP-GLU-340 AND
RP 375-SER-ALA-376.
RX PubMed=9461305; DOI=10.1111/j.1432-1033.1997.00800.x;
RA Valdez B.C., Henning D., Perumal K., Busch H.;
RT "RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two
RT activities in separate domains of the same protein.";
RL Eur. J. Biochem. 250:800-807(1997).
RN [11]
RP FUNCTION.
RX PubMed=14559904; DOI=10.1074/jbc.m310846200;
RA Henning D., So R.B., Jin R., Lau L.F., Valdez B.C.;
RT "Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA
RT production.";
RL J. Biol. Chem. 278:52307-52314(2003).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [14]
RP IDENTIFICATION IN THE B-WICH COMPLEX.
RX PubMed=16603771; DOI=10.1074/jbc.m600233200;
RA Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.;
RT "The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear
RT proteins in transcription.";
RL J. Biol. Chem. 281:16264-16271(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=18180292; DOI=10.1074/jbc.m709613200;
RA Holmstrom T.H., Mialon A., Kallio M., Nymalm Y., Mannermaa L., Holm T.,
RA Johansson H., Black E., Gillespie D., Salminen T.A., Langel U.,
RA Valdez B.C., Westermarck J.;
RT "c-Jun supports ribosomal RNA processing and nucleolar localization of RNA
RT helicase DDX21.";
RL J. Biol. Chem. 283:7046-7053(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71 AND SER-89, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-121, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71; SER-89; SER-121;
RP THR-296 AND SER-567, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [23]
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 [24]
RP INTERACTION WITH C1QBP.
RX PubMed=21536856; DOI=10.1074/mcp.m110.006148;
RA Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K.,
RA Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T.,
RA Takahashi N.;
RT "Splicing factor 2-associated protein p32 participates in ribosome
RT biogenesis by regulating the binding of Nop52 and fibrillarin to
RT preribosome particles.";
RL Mol. Cell. Proteomics 10:0-0(2011).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71; SER-89 AND
RP SER-121, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [27]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH WDR46.
RX PubMed=23848194; DOI=10.1111/gtc.12077;
RA Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T.,
RA Takeyasu K.;
RT "Nucleolar scaffold protein, WDR46, determines the granular compartmental
RT localization of nucleolin and DDX21.";
RL Genes Cells 18:780-797(2013).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-13; SER-71; SER-89;
RP SER-121; THR-296 AND SER-567, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [29]
RP INTERACTION WITH MCM3AP.
RX PubMed=23652018; DOI=10.1038/ncomms2823;
RA Singh S.K., Maeda K., Eid M.M., Almofty S.A., Ono M., Pham P.,
RA Goodman M.F., Sakaguchi N.;
RT "GANP regulates recruitment of AID to immunoglobulin variable regions by
RT modulating transcription and nucleosome occupancy.";
RL Nat. Commun. 4:1830-1830(2013).
RN [30]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25260534; DOI=10.1186/s13058-014-0449-z;
RA Zhang Y., Baysac K.C., Yee L.F., Saporita A.J., Weber J.D.;
RT "Elevated DDX21 regulates c-Jun activity and rRNA processing in human
RT breast cancers.";
RL Breast Cancer Res. 16:449-449(2014).
RN [31]
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 [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [33]
RP FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP 339-ASP-GLU-340 AND 375-SER-ALA-376.
RX PubMed=25470060; DOI=10.1038/nature13923;
RA Calo E., Flynn R.A., Martin L., Spitale R.C., Chang H.Y., Wysocka J.;
RT "RNA helicase DDX21 coordinates transcription and ribosomal RNA
RT processing.";
RL Nature 518:249-253(2015).
RN [34]
RP FUNCTION, AND RNA-BINDING.
RX PubMed=25477391; DOI=10.1093/nar/gku1291;
RA Sloan K.E., Leisegang M.S., Doebele C., Ramirez A.S., Simm S.,
RA Safferthal C., Kretschmer J., Schorge T., Markoutsa S., Haag S., Karas M.,
RA Ebersberger I., Schleiff E., Watkins N.J., Bohnsack M.T.;
RT "The association of late-acting snoRNPs with human pre-ribosomal complexes
RT requires the RNA helicase DDX21.";
RL Nucleic Acids Res. 43:553-564(2015).
RN [35]
RP FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-18; LYS-137 AND LYS-600,
RP AND MUTAGENESIS OF LYS-18; LYS-137; 339-ASP-GLU-340; 375-SER-ALA-376 AND
RP LYS-600.
RX PubMed=28790157; DOI=10.1101/gad.300624.117;
RA Song C., Hotz-Wagenblatt A., Voit R., Grummt I.;
RT "SIRT7 and the DEAD-box helicase DDX21 cooperate to resolve genomic R loops
RT and safeguard genome stability.";
RL Genes Dev. 31:1370-1381(2017).
RN [36]
RP FUNCTION, AND MIRNA-BINDING.
RX PubMed=28431233; DOI=10.1016/j.molcel.2017.03.014;
RA Treiber T., Treiber N., Plessmann U., Harlander S., Daiss J.L., Eichner N.,
RA Lehmann G., Schall K., Urlaub H., Meister G.;
RT "A Compendium of RNA-Binding Proteins that Regulate MicroRNA Biogenesis.";
RL Mol. Cell 66:270-284(2017).
RN [37]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP 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 [38]
RP STRUCTURE BY NMR OF 617-710.
RA Dutta S.K., Serrano P., Geralt M., Wuthrich K.;
RT "NMR structure of the GUCT domain from human DEAD box polypeptide 21
RT (DDX21).";
RL Submitted (JAN-2013) to the PDB data bank.
CC -!- FUNCTION: RNA helicase that acts as a sensor of the transcriptional
CC status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA
CC (rRNA) processing and transcription from polymerase II (Pol II)
CC (PubMed:25470060, PubMed:28790157). Binds various RNAs, such as rRNAs,
CC snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the
CC nucleolus, localizes to rDNA locus, where it directly binds rRNAs and
CC snoRNAs, and promotes rRNA transcription, processing and modification.
CC Required for rRNA 2'-O-methylation, possibly by promoting the
CC recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-
CC ribosomal complexes (PubMed:25470060, PubMed:25477391). In the
CC nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-
CC transcribed genes: acts by facilitating the release of P-TEFb from
CC inhibitory 7SK snRNP in a manner that is dependent on its helicase
CC activity, thereby promoting transcription of its target genes
CC (PubMed:25470060). Functions as cofactor for JUN-activated
CC transcription: required for phosphorylation of JUN at 'Ser-77'
CC (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA
CC (helicase) and can fold or introduce a secondary structure to a single-
CC stranded RNA (foldase) (PubMed:9461305). Together with SIRT7, required
CC to prevent R-loop-associated DNA damage and transcription-associated
CC genomic instability: deacetylation by SIRT7 activates the helicase
CC activity, thereby overcoming R-loop-mediated stalling of RNA
CC polymerases (PubMed:28790157). Involved in rRNA processing
CC (PubMed:14559904, PubMed:18180292). May bind to specific miRNA hairpins
CC (PubMed:28431233). Component of a multi-helicase-TICAM1 complex that
CC acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and
CC plays a role in the activation of a cascade of antiviral responses
CC including the induction of pro-inflammatory cytokines via the adapter
CC molecule TICAM1 (By similarity). {ECO:0000250|UniProtKB:Q9JIK5,
CC ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:14559904,
CC ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:25260534,
CC ECO:0000269|PubMed:25470060, ECO:0000269|PubMed:25477391,
CC ECO:0000269|PubMed:28431233, ECO:0000269|PubMed:28790157,
CC ECO:0000269|PubMed:9461305}.
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=3.6.4.13;
CC Evidence={ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305};
CC -!- ACTIVITY REGULATION: Acetylation inhibits the helicase activity.
CC {ECO:0000269|PubMed:28790157}.
CC -!- SUBUNIT: Homodimer; homodimerizes via its N-terminus. Found in a multi-
CC helicase-TICAM1 complex at least composed of DHX36, DDX1, DDX21 and
CC TICAM1; this complex exists in resting cells with or without poly(I:C)
CC RNA ligand stimulation. Interacts (via C-terminus) with TICAM1 (via TIR
CC domain). Interacts with DHX36 (via C-terminus); this interaction serves
CC as bridges to TICAM1. Interacts (via C-terminus) with DDX1 (via
CC B30.2/SPRY domain); this interaction serves as bridges to TICAM1.
CC Component of the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with
CC C1QBP. Interacts with JUN. Interacts with WDR46 (By similarity).
CC Component of the B-WICH complex, at least composed of SMARCA5/SNF2H,
CC BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with
CC C1QBP. Interacts with JUN (PubMed:11823437, PubMed:18180292). Interacts
CC with WDR46 (PubMed:23848194). Interacts with MCM3AP isoform GANP
CC (PubMed:23652018). Interacts with WDR43 (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437,
CC ECO:0000269|PubMed:16603771, ECO:0000269|PubMed:18180292,
CC ECO:0000269|PubMed:21536856, ECO:0000269|PubMed:23652018,
CC ECO:0000269|PubMed:23848194}.
CC -!- INTERACTION:
CC Q9NR30; Q8N187: CARF; NbExp=3; IntAct=EBI-357942, EBI-745541;
CC Q9NR30; P07910: HNRNPC; NbExp=3; IntAct=EBI-357942, EBI-357966;
CC Q9NR30; P42858: HTT; NbExp=3; IntAct=EBI-357942, EBI-466029;
CC Q9NR30; O00505: KPNA3; NbExp=3; IntAct=EBI-357942, EBI-358297;
CC Q9NR30; Q99732: LITAF; NbExp=3; IntAct=EBI-357942, EBI-725647;
CC Q9NR30; P10636: MAPT; NbExp=3; IntAct=EBI-357942, EBI-366182;
CC Q9NR30; Q15554: TERF2; NbExp=2; IntAct=EBI-357942, EBI-706637;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:11823437,
CC ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194,
CC ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060,
CC ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:8614622}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:11823437, ECO:0000269|PubMed:18180292,
CC ECO:0000269|PubMed:25260534, ECO:0000269|PubMed:25470060,
CC ECO:0000269|PubMed:28790157}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q9JIK5}. Note=Present both in nucleolus and
CC nucleoplasm. Interaction with JUN promotes translocation from the
CC nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292).
CC Interaction with WDR46 is required for localization to the nucleolus
CC (PubMed:23848194). Colocalizes in the cytosol with DDX1, DHX36 and
CC TICAM1. The multi-helicase-TICAM1 complex may translocate to the
CC mitochondria upon poly(I:C) RNA ligand stimulation (By similarity).
CC {ECO:0000250|UniProtKB:Q9JIK5, ECO:0000269|PubMed:11823437,
CC ECO:0000269|PubMed:18180292, ECO:0000269|PubMed:23848194}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NR30-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NR30-2; Sequence=VSP_015716;
CC -!- DOMAIN: The helicase and foldase activities reside in two separate
CC domains, the helicase in the N-terminus and the foldase in the C-
CC terminus. {ECO:0000269|PubMed:9461305}.
CC -!- DOMAIN: The 3 X 5 AA repeats seem to be critical for the RNA folding
CC activity. {ECO:0000250}.
CC -!- PTM: Acetylation by CREBBP/CBP inhibits the helicase activity
CC (PubMed:28790157). Deacetylation by SIRT7 promotes the helicase
CC activity and overcomes R-loop-mediated stalling of RNA polymerases
CC (PubMed:28790157). {ECO:0000269|PubMed:28790157}.
CC -!- MISCELLANEOUS: Autoantibodies against DDX21 are found in patients with
CC watermelon stomach disease, which is characterized by prominent stripes
CC of ectatic vascular tissue in the stomach similar to stripes on a
CC watermelon. {ECO:0000269|PubMed:8614622}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX21/DDX50
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB02546.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U41387; AAB02546.1; ALT_INIT; mRNA.
DR EMBL; AF261903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF261917; AAF78930.2; -; Genomic_DNA.
DR EMBL; AF261904; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261905; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261906; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261907; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261908; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261909; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261910; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261911; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261912; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261913; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261914; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261915; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AF261916; AAF78930.2; JOINED; Genomic_DNA.
DR EMBL; AK315585; BAG37957.1; -; mRNA.
DR EMBL; CR749598; CAH18395.1; -; mRNA.
DR EMBL; AL359844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471083; EAW54307.1; -; Genomic_DNA.
DR EMBL; BC008071; AAH08071.2; -; mRNA.
DR CCDS; CCDS31211.1; -. [Q9NR30-1]
DR CCDS; CCDS73144.1; -. [Q9NR30-2]
DR PIR; PC6010; PC6010.
DR RefSeq; NP_001243839.1; NM_001256910.1. [Q9NR30-2]
DR RefSeq; NP_004719.2; NM_004728.3. [Q9NR30-1]
DR PDB; 2M3D; NMR; -; A=617-710.
DR PDB; 6L5L; X-ray; 3.10 A; A=188-563.
DR PDB; 6L5M; X-ray; 2.70 A; A/B/C/D/E=188-563.
DR PDB; 6L5N; X-ray; 2.24 A; A/B=188-563.
DR PDB; 6L5O; X-ray; 1.80 A; A=188-563.
DR PDBsum; 2M3D; -.
DR PDBsum; 6L5L; -.
DR PDBsum; 6L5M; -.
DR PDBsum; 6L5N; -.
DR PDBsum; 6L5O; -.
DR AlphaFoldDB; Q9NR30; -.
DR BMRB; Q9NR30; -.
DR SASBDB; Q9NR30; -.
DR SMR; Q9NR30; -.
DR BioGRID; 114625; 544.
DR ComplexPortal; CPX-1099; B-WICH chromatin remodelling complex.
DR CORUM; Q9NR30; -.
DR DIP; DIP-32941N; -.
DR IntAct; Q9NR30; 137.
DR MINT; Q9NR30; -.
DR STRING; 9606.ENSP00000346120; -.
DR ChEMBL; CHEMBL4296016; -.
DR GlyGen; Q9NR30; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q9NR30; -.
DR MetOSite; Q9NR30; -.
DR PhosphoSitePlus; Q9NR30; -.
DR SwissPalm; Q9NR30; -.
DR BioMuta; DDX21; -.
DR DMDM; 76803555; -.
DR SWISS-2DPAGE; Q9NR30; -.
DR CPTAC; CPTAC-494; -.
DR CPTAC; CPTAC-495; -.
DR EPD; Q9NR30; -.
DR jPOST; Q9NR30; -.
DR MassIVE; Q9NR30; -.
DR MaxQB; Q9NR30; -.
DR PaxDb; Q9NR30; -.
DR PeptideAtlas; Q9NR30; -.
DR PRIDE; Q9NR30; -.
DR ProteomicsDB; 82265; -. [Q9NR30-1]
DR ProteomicsDB; 82266; -. [Q9NR30-2]
DR TopDownProteomics; Q9NR30-1; -. [Q9NR30-1]
DR Antibodypedia; 14684; 273 antibodies from 26 providers.
DR DNASU; 9188; -.
DR Ensembl; ENST00000354185.9; ENSP00000346120.4; ENSG00000165732.14. [Q9NR30-1]
DR Ensembl; ENST00000620315.2; ENSP00000480334.1; ENSG00000165732.14. [Q9NR30-2]
DR Ensembl; ENST00000690316.1; ENSP00000510035.1; ENSG00000165732.14. [Q9NR30-2]
DR GeneID; 9188; -.
DR KEGG; hsa:9188; -.
DR MANE-Select; ENST00000354185.9; ENSP00000346120.4; NM_004728.4; NP_004719.2.
DR UCSC; uc001jov.3; human. [Q9NR30-1]
DR CTD; 9188; -.
DR DisGeNET; 9188; -.
DR GeneCards; DDX21; -.
DR HGNC; HGNC:2744; DDX21.
DR HPA; ENSG00000165732; Low tissue specificity.
DR MIM; 606357; gene.
DR neXtProt; NX_Q9NR30; -.
DR OpenTargets; ENSG00000165732; -.
DR PharmGKB; PA27210; -.
DR VEuPathDB; HostDB:ENSG00000165732; -.
DR eggNOG; KOG0331; Eukaryota.
DR GeneTree; ENSGT00940000155043; -.
DR HOGENOM; CLU_003041_20_0_1; -.
DR InParanoid; Q9NR30; -.
DR OMA; KQVHTDF; -.
DR OrthoDB; 1139373at2759; -.
DR PhylomeDB; Q9NR30; -.
DR TreeFam; TF328622; -.
DR BRENDA; 3.6.4.13; 2681.
DR PathwayCommons; Q9NR30; -.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR SignaLink; Q9NR30; -.
DR SIGNOR; Q9NR30; -.
DR BioGRID-ORCS; 9188; 673 hits in 1091 CRISPR screens.
DR ChiTaRS; DDX21; human.
DR GeneWiki; DDX21; -.
DR GenomeRNAi; 9188; -.
DR Pharos; Q9NR30; Tbio.
DR PRO; PR:Q9NR30; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NR30; protein.
DR Bgee; ENSG00000165732; Expressed in pericardium and 207 other tissues.
DR Genevisible; Q9NR30; HS.
DR GO; GO:0110016; C:B-WICH complex; IDA:ComplexPortal.
DR GO; GO:0005694; C:chromosome; IDA:HPA.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0097322; F:7SK snRNA binding; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003725; F:double-stranded RNA binding; IEA:Ensembl.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0035198; F:miRNA binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IDA:UniProtKB.
DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IC:ComplexPortal.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0001649; P:osteoblast differentiation; HDA:UniProtKB.
DR GO; GO:0035066; P:positive regulation of histone acetylation; IC:ComplexPortal.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISS:UniProtKB.
DR GO; GO:0002735; P:positive regulation of myeloid dendritic cell cytokine production; IEA:Ensembl.
DR GO; GO:0045943; P:positive regulation of transcription by RNA polymerase I; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IC:ComplexPortal.
DR GO; GO:0045945; P:positive regulation of transcription by RNA polymerase III; IDA:ComplexPortal.
DR GO; GO:0062176; P:R-loop disassembly; IDA:UniProtKB.
DR GO; GO:0043330; P:response to exogenous dsRNA; IEA:Ensembl.
DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR012562; GUCT.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR035979; RBD_domain_sf.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF08152; GUCT; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51195; Q_MOTIF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Antiviral defense;
KW ATP-binding; Cytoplasm; Direct protein sequencing; Helicase; Hydrolase;
KW Immunity; Innate immunity; Isopeptide bond; Mitochondrion;
KW Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW RNA-binding; rRNA processing; Transcription; Ubl conjugation.
FT CHAIN 1..783
FT /note="Nucleolar RNA helicase 2"
FT /id="PRO_0000055027"
FT DOMAIN 217..396
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 429..573
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REPEAT 724..728
FT /note="1"
FT REPEAT 734..738
FT /note="2"
FT REPEAT 744..748
FT /note="3"
FT REGION 1..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..783
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 724..748
FT /note="3 X 5 AA repeats"
FT MOTIF 186..214
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 339..342
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 11..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 731..752
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 758..783
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 18
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:28790157"
FT MOD_RES 71
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 89
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 121
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 137
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:28790157"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 164
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 171
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9JIK5"
FT MOD_RES 296
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 600
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:28790157"
FT MOD_RES 779
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_015716"
FT VARIANT 27
FT /note="T -> I (in dbSNP:rs17556220)"
FT /evidence="ECO:0000269|PubMed:11237763,
FT ECO:0000269|PubMed:8614622"
FT /id="VAR_052161"
FT MUTAGEN 18
FT /note="K->Q: Mimics acetylation; impaired ability to
FT resolve R-loops; when associated with Q-137 and Q-600."
FT /evidence="ECO:0000269|PubMed:28790157"
FT MUTAGEN 137
FT /note="K->Q: Mimics acetylation; impaired ability to
FT resolve R-loops; when associated with Q-18 and Q-600."
FT /evidence="ECO:0000269|PubMed:28790157"
FT MUTAGEN 339..340
FT /note="DE->HG: In mutant DEV; loss of helicase activity.
FT Defects in release of P-TEFb from inhibitory 7SK snRNP."
FT /evidence="ECO:0000269|PubMed:25470060,
FT ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305"
FT MUTAGEN 375..376
FT /note="SA->LE: In mutant SAT; ATPase defective. Defects in
FT release of P-TEFb from inhibitory 7SK snRNP."
FT /evidence="ECO:0000269|PubMed:25470060,
FT ECO:0000269|PubMed:28790157, ECO:0000269|PubMed:9461305"
FT MUTAGEN 600
FT /note="K->Q: Mimics acetylation; impaired ability to
FT resolve R-loops; when associated with Q-18 and Q-137."
FT /evidence="ECO:0000269|PubMed:28790157"
FT CONFLICT 273
FT /note="A -> C (in Ref. 2; AAF78930)"
FT /evidence="ECO:0000305"
FT HELIX 195..203
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 211..221
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 236..251
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 262..266
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 270..283
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 285..287
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 316..324
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 334..339
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 341..346
FT /evidence="ECO:0007829|PDB:6L5O"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6L5N"
FT HELIX 350..360
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 370..376
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 380..386
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 387..389
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 395..400
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:6L5N"
FT STRAND 411..417
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 423..434
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 441..446
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 448..456
FT /evidence="ECO:0007829|PDB:6L5O"
FT TURN 458..460
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 461..463
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 464..467
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 473..484
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 489..494
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 495..498
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 506..513
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 535..541
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 543..545
FT /evidence="ECO:0007829|PDB:6L5O"
FT HELIX 546..556
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 561..563
FT /evidence="ECO:0007829|PDB:6L5O"
FT STRAND 631..642
FT /evidence="ECO:0007829|PDB:2M3D"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:2M3D"
FT TURN 664..667
FT /evidence="ECO:0007829|PDB:2M3D"
FT HELIX 676..678
FT /evidence="ECO:0007829|PDB:2M3D"
FT STRAND 679..686
FT /evidence="ECO:0007829|PDB:2M3D"
FT HELIX 687..693
FT /evidence="ECO:0007829|PDB:2M3D"
FT STRAND 704..707
FT /evidence="ECO:0007829|PDB:2M3D"
FT MOD_RES Q9NR30-2:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
SQ SEQUENCE 783 AA; 87344 MW; 4F6673E38686644F CRC64;
MPGKLRSDAG LESDTAMKKG ETLRKQTEEK EKKEKPKSDK TEEIAEEEET VFPKAKQVKK
KAEPSEVDMN SPKSKKAKKK EEPSQNDISP KTKSLRKKKE PIEKKVVSSK TKKVTKNEEP
SEEEIDAPKP KKMKKEKEMN GETREKSPKL KNGFPHPEPD CNPSEAASEE SNSEIEQEIP
VEQKEGAFSN FPISEETIKL LKGRGVTFLF PIQAKTFHHV YSGKDLIAQA RTGTGKTFSF
AIPLIEKLHG ELQDRKRGRA PQVLVLAPTR ELANQVSKDF SDITKKLSVA CFYGGTPYGG
QFERMRNGID ILVGTPGRIK DHIQNGKLDL TKLKHVVLDE VDQMLDMGFA DQVEEILSVA
YKKDSEDNPQ TLLFSATCPH WVFNVAKKYM KSTYEQVDLI GKKTQKTAIT VEHLAIKCHW
TQRAAVIGDV IRVYSGHQGR TIIFCETKKE AQELSQNSAI KQDAQSLHGD IPQKQREITL
KGFRNGSFGV LVATNVAARG LDIPEVDLVI QSSPPKDVES YIHRSGRTGR AGRTGVCICF
YQHKEEYQLV QVEQKAGIKF KRIGVPSATE IIKASSKDAI RLLDSVPPTA ISHFKQSAEK
LIEEKGAVEA LAAALAHISG ATSVDQRSLI NSNVGFVTMI LQCSIEMPNI SYAWKELKEQ
LGEEIDSKVK GMVFLKGKLG VCFDVPTASV TEIQEKWHDS RRWQLSVATE QPELEGPREG
YGGFRGQREG SRGFRGQRDG NRRFRGQREG SRGPRGQRSG GGNKSNRSQN KGQKRSFSKA
FGQ
