DDX23_HUMAN
ID DDX23_HUMAN Reviewed; 820 AA.
AC Q9BUQ8; B2R600; B4DH15; O43188;
DT 07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-OCT-2007, sequence version 3.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX23 {ECO:0000305};
DE EC=3.6.4.13 {ECO:0000305};
DE AltName: Full=100 kDa U5 snRNP-specific protein;
DE AltName: Full=DEAD box protein 23;
DE AltName: Full=PRP28 homolog;
DE AltName: Full=U5-100kD;
GN Name=DDX23 {ECO:0000312|HGNC:HGNC:17347};
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), PROTEIN SEQUENCE OF 272-290;
RP 409-419 AND 433-441, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP IDENTIFICATION IN U5 AND U5/4/6 SNRNP COMPLEXES.
RX PubMed=9409622;
RA Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.;
RT "The human U5 snRNP-specific 100-kD protein is an RS domain-containing,
RT putative RNA helicase with significant homology to the yeast splicing
RT factor Prp28p.";
RL RNA 3:1313-1326(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Amygdala, and Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
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 [8]
RP SUBUNIT.
RX PubMed=16723661; DOI=10.1261/rna.55406;
RA Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.;
RT "The network of protein-protein interactions within the human U4/U6.U5 tri-
RT snRNP.";
RL RNA 12:1418-1430(2006).
RN [9]
RP FUNCTION, AND PHOSPHORYLATION BY SRPK2.
RX PubMed=18425142; DOI=10.1038/nsmb.1415;
RA Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R., Luehrmann R.;
RT "Phosphorylation of human PRP28 by SRPK2 is required for integration of the
RT U4/U6-U5 tri-snRNP into the spliceosome.";
RL Nat. Struct. Mol. Biol. 15:435-443(2008).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, AND
RP SUBCELLULAR LOCATION.
RX PubMed=20858735; DOI=10.1158/1541-7786.mcr-10-0042;
RA Gilmore-Hebert M., Ramabhadran R., Stern D.F.;
RT "Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage
RT response pathways.";
RL Mol. Cancer Res. 8:1388-1398(2010).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-107 AND SER-109, AND
RP 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 [14]
RP IDENTIFICATION 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 [15]
RP INTERACTION WITH ERCC6.
RX PubMed=26030138; DOI=10.1371/journal.pone.0128558;
RA Nicolai S., Filippi S., Caputo M., Cipak L., Gregan J., Ammerer G.,
RA Frontini M., Willems D., Prantera G., Balajee A.S., Proietti-De-Santis L.;
RT "Identification of Novel Proteins Co-Purifying with Cockayne Syndrome Group
RT B (CSB) Reveals Potential Roles for CSB in RNA Metabolism and Chromatin
RT Dynamics.";
RL PLoS ONE 10:E0128558-E0128558(2015).
RN [16]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND PHOSPHORYLATION.
RX PubMed=28076779; DOI=10.1016/j.celrep.2016.12.050;
RA Sridhara S.C., Carvalho S., Grosso A.R., Gallego-Paez L.M.,
RA Carmo-Fonseca M., de Almeida S.F.;
RT "Transcription Dynamics Prevent RNA-Mediated Genomic Instability through
RT SRPK2-Dependent DDX23 Phosphorylation.";
RL Cell Rep. 18:334-343(2017).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-686 AND LYS-811, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in pre-mRNA splicing and its phosphorylated form (by
CC SRPK2) is required for spliceosomal B complex formation
CC (PubMed:18425142). Independently of its spliceosome formation function,
CC required for the suppression of incorrect R-loops formed during
CC transcription; R-loops are composed of a DNA:RNA hybrid and the
CC associated non-template single-stranded DNA (PubMed:28076779).
CC {ECO:0000269|PubMed:18425142, ECO:0000269|PubMed:28076779}.
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:0000305};
CC -!- SUBUNIT: The phosphorylated form (by SRPK2) is a component of the
CC U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at
CC least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57,
CC SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and USP39
CC (PubMed:16723661, PubMed:9409622). Identified in the spliceosome C
CC complex (PubMed:11991638). Interacts with ERBB4 (PubMed:20858735).
CC Interacts with ERCC6 (PubMed:26030138). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:16723661, ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:26030138, ECO:0000269|PubMed:9409622}.
CC -!- INTERACTION:
CC Q9BUQ8; Q96DI7: SNRNP40; NbExp=2; IntAct=EBI-540096, EBI-538492;
CC Q9BUQ8; P54274: TERF1; NbExp=2; IntAct=EBI-540096, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9409622}. Chromosome
CC {ECO:0000269|PubMed:28076779}. Note=During transcription, accumulates
CC at chromatin loci where unscheduled R-loops form and colocalizes with
CC paused 'Ser-5'-phosphorlyated POLR2A/RNA polymerase II and kinase
CC SRPK2. {ECO:0000269|PubMed:28076779}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9BUQ8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BUQ8-2; Sequence=VSP_056575, VSP_056576;
CC -!- PTM: In vitro phosphorylated by CLK1 and U1 snRNP-associated protein
CC kinase (PubMed:9409622). Phosphorylated by SRPK2 and this
CC phosphorylation is required for its association with the tri-snRNP
CC (U4/U6-U5 tri-small nuclear ribonucleoproteins) and subsequent
CC spliceosomal B complex formation (PubMed:18425142). May be
CC phosphorylated by SRPK2 on Ser residues in the SR domain; the
CC phosphorylation is required for the removal of inappropriate R-loops
CC during transcription (PubMed:28076779). {ECO:0000269|PubMed:18425142,
CC ECO:0000269|PubMed:28076779, ECO:0000269|PubMed:9409622}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000305}.
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DR EMBL; AF026402; AAB87902.1; -; mRNA.
DR EMBL; AK294877; BAG57976.1; -; mRNA.
DR EMBL; AK312379; BAG35297.1; -; mRNA.
DR EMBL; AC117498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471111; EAW58011.1; -; Genomic_DNA.
DR EMBL; BC002366; AAH02366.1; -; mRNA.
DR CCDS; CCDS8770.1; -. [Q9BUQ8-1]
DR RefSeq; NP_004809.2; NM_004818.2. [Q9BUQ8-1]
DR PDB; 3JCR; EM; 7.00 A; F=1-820.
DR PDB; 4NHO; X-ray; 2.00 A; A=338-820.
DR PDB; 6AH0; EM; 5.70 A; X=1-820.
DR PDB; 6QW6; EM; 2.92 A; 5X=1-820.
DR PDB; 6QX9; EM; 3.28 A; 5X=1-820.
DR PDBsum; 3JCR; -.
DR PDBsum; 4NHO; -.
DR PDBsum; 6AH0; -.
DR PDBsum; 6QW6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; Q9BUQ8; -.
DR SMR; Q9BUQ8; -.
DR BioGRID; 114811; 404.
DR ComplexPortal; CPX-2391; U4/U6.U5 small nuclear ribonucleoprotein complex.
DR CORUM; Q9BUQ8; -.
DR DIP; DIP-34974N; -.
DR IntAct; Q9BUQ8; 73.
DR MINT; Q9BUQ8; -.
DR STRING; 9606.ENSP00000310723; -.
DR GlyGen; Q9BUQ8; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BUQ8; -.
DR MetOSite; Q9BUQ8; -.
DR PhosphoSitePlus; Q9BUQ8; -.
DR SwissPalm; Q9BUQ8; -.
DR BioMuta; DDX23; -.
DR DMDM; 160385708; -.
DR EPD; Q9BUQ8; -.
DR jPOST; Q9BUQ8; -.
DR MassIVE; Q9BUQ8; -.
DR MaxQB; Q9BUQ8; -.
DR PaxDb; Q9BUQ8; -.
DR PeptideAtlas; Q9BUQ8; -.
DR PRIDE; Q9BUQ8; -.
DR ProteomicsDB; 4180; -.
DR ProteomicsDB; 79121; -. [Q9BUQ8-1]
DR Antibodypedia; 13695; 204 antibodies from 24 providers.
DR DNASU; 9416; -.
DR Ensembl; ENST00000308025.8; ENSP00000310723.2; ENSG00000174243.10. [Q9BUQ8-1]
DR Ensembl; ENST00000547135.5; ENSP00000446770.1; ENSG00000174243.10. [Q9BUQ8-2]
DR GeneID; 9416; -.
DR KEGG; hsa:9416; -.
DR MANE-Select; ENST00000308025.8; ENSP00000310723.2; NM_004818.3; NP_004809.2.
DR UCSC; uc001rsm.4; human. [Q9BUQ8-1]
DR CTD; 9416; -.
DR DisGeNET; 9416; -.
DR GeneCards; DDX23; -.
DR HGNC; HGNC:17347; DDX23.
DR HPA; ENSG00000174243; Low tissue specificity.
DR MIM; 612172; gene.
DR neXtProt; NX_Q9BUQ8; -.
DR OpenTargets; ENSG00000174243; -.
DR PharmGKB; PA134934941; -.
DR VEuPathDB; HostDB:ENSG00000174243; -.
DR eggNOG; KOG0333; Eukaryota.
DR GeneTree; ENSGT00940000155606; -.
DR HOGENOM; CLU_003041_11_0_1; -.
DR InParanoid; Q9BUQ8; -.
DR OMA; KKFNFEW; -.
DR PhylomeDB; Q9BUQ8; -.
DR TreeFam; TF300527; -.
DR PathwayCommons; Q9BUQ8; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR SignaLink; Q9BUQ8; -.
DR BioGRID-ORCS; 9416; 643 hits in 1085 CRISPR screens.
DR ChiTaRS; DDX23; human.
DR GeneWiki; DDX23; -.
DR GenomeRNAi; 9416; -.
DR Pharos; Q9BUQ8; Tbio.
DR PRO; PR:Q9BUQ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9BUQ8; protein.
DR Bgee; ENSG00000174243; Expressed in calcaneal tendon and 199 other tissues.
DR ExpressionAtlas; Q9BUQ8; baseline and differential.
DR Genevisible; Q9BUQ8; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046540; C:U4/U6 x U5 tri-snRNP complex; IDA:MGI.
DR GO; GO:0005682; C:U5 snRNP; IDA:HGNC-UCL.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; TAS:ProtInc.
DR GO; GO:0000354; P:cis assembly of pre-catalytic spliceosome; IC:HGNC-UCL.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0062176; P:R-loop disassembly; IDA:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
DR DisProt; DP02332; -.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS.
DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif.
DR Pfam; PF00270; DEAD; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS00039; DEAD_ATP_HELICASE; 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; Alternative splicing; ATP-binding; Chromosome;
KW Direct protein sequencing; Helicase; Hydrolase; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..820
FT /note="Probable ATP-dependent RNA helicase DDX23"
FT /id="PRO_0000055128"
FT DOMAIN 422..627
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 651..799
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..244
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 391..419
FT /note="Q motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00552"
FT MOTIF 549..552
FT /note="DEAD box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT COMPBIAS 1..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..61
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 62..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 435..442
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 109
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 686
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 811
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 107..108
FT /note="SL -> RH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056575"
FT VAR_SEQ 109..820
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056576"
FT CONFLICT 137
FT /note="P -> L (in Ref. 1; AAB87902)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="D -> E (in Ref. 1; AAB87902)"
FT /evidence="ECO:0000305"
FT CONFLICT 309
FT /note="L -> F (in Ref. 1; AAB87902)"
FT /evidence="ECO:0000305"
FT HELIX 357..359
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:4NHO"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 400..409
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 416..425
FT /evidence="ECO:0007829|PDB:4NHO"
FT TURN 426..428
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 431..434
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 441..455
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 458..461
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 470..474
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 478..492
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 493..495
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 499..502
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 508..516
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 520..524
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 526..534
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 545..550
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 551..556
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 560..567
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 572..574
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 580..583
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 585..593
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 611..620
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 625..629
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 635..638
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 639..645
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 648..650
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 651..660
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 667..670
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 674..686
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 691..693
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 704..712
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 717..720
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 734..740
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 745..752
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 753..755
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 757..760
FT /evidence="ECO:0007829|PDB:4NHO"
FT STRAND 763..768
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 770..775
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 776..784
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 793..796
FT /evidence="ECO:0007829|PDB:4NHO"
FT HELIX 799..801
FT /evidence="ECO:0007829|PDB:4NHO"
SQ SEQUENCE 820 AA; 95583 MW; 01DD5BCF8BFBA2DB CRC64;
MAGELADKKD RDASPSKEER KRSRTPDRER DRDRDRKSSP SKDRKRHRSR DRRRGGSRSR
SRSRSKSAER ERRHKERERD KERDRNKKDR DRDKDGHRRD KDRKRSSLSP GRGKDFKSRK
DRDSKKDEED EHGDKKPKAQ PLSLEELLAK KKAEEEAEAK PKFLSKAERE AEALKRRQQE
VEERQRMLEE ERKKRKQFQD LGRKMLEDPQ ERERRERRER MERETNGNED EEGRQKIREE
KDKSKELHAI KERYLGGIKK RRRTRHLNDR KFVFEWDASE DTSIDYNPLY KERHQVQLLG
RGFIAGIDLK QQKREQSRFY GDLMEKRRTL EEKEQEEARL RKLRKKEAKQ RWDDRHWSQK
KLDEMTDRDW RIFREDYSIT TKGGKIPNPI RSWKDSSLPP HILEVIDKCG YKEPTPIQRQ
AIPIGLQNRD IIGVAETGSG KTAAFLIPLL VWITTLPKID RIEESDQGPY AIILAPTREL
AQQIEEETIK FGKPLGIRTV AVIGGISRED QGFRLRMGCE IVIATPGRLI DVLENRYLVL
SRCTYVVLDE ADRMIDMGFE PDVQKILEHM PVSNQKPDTD EAEDPEKMLA NFESGKHKYR
QTVMFTATMP PAVERLARSY LRRPAVVYIG SAGKPHERVE QKVFLMSESE KRKKLLAILE
QGFDPPIIIF VNQKKGCDVL AKSLEKMGYN ACTLHGGKGQ EQREFALSNL KAGAKDILVA
TDVAGRGIDI QDVSMVVNYD MAKNIEDYIH RIGRTGRAGK SGVAITFLTK EDSAVFYELK
QAILESPVSS CPPELANHPD AQHKPGTILT KKRREETIFA
