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 27-MAR-2024, entry version 200. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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 EMDB; EMD-4658; -. DR EMDB; EMD-4665; -. DR EMDB; EMD-9621; -. DR SMR; Q9BUQ8; -. DR BioGRID; 114811; 468. 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; 9606-ENSP00000310723; -. DR PeptideAtlas; Q9BUQ8; -. DR ProteomicsDB; 4180; -. DR ProteomicsDB; 79121; -. [Q9BUQ8-1] DR Pumba; Q9BUQ8; -. DR Antibodypedia; 13695; 222 antibodies from 24 providers. DR DNASU; 9416; -. DR Ensembl; ENST00000308025.8; ENSP00000310723.2; ENSG00000174243.11. [Q9BUQ8-1] DR Ensembl; ENST00000547135.5; ENSP00000446770.1; ENSG00000174243.11. [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 AGR; HGNC:17347; -. 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; ARDIKHM; -. DR OrthoDB; 5487240at2759; -. 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 SIGNOR; Q9BUQ8; -. DR BioGRID-ORCS; 9416; 675 hits in 1166 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 201 other cell types or tissues. DR ExpressionAtlas; Q9BUQ8; baseline and differential. 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:Reactome. 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 processing; IDA:UniProtKB. DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc. DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB. DR CDD; cd17945; DEADc_DDX23; 1. DR CDD; cd18787; SF2_C_DEAD; 1. DR DisProt; DP02332; -. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR47958; ATP-DEPENDENT RNA HELICASE DBP3; 1. DR PANTHER; PTHR47958:SF56; RNA HELICASE; 1. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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. DR Genevisible; Q9BUQ8; HS. 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 //