MyHits has reached its end of life and no longer provides data or services. Thank you for your support and trust for more than 23 years!
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
However, the webserver will remain online in its present form at least until end of March 2025.
To ensure the future of MyHits, we would be happy if a person or community would take over the resource or parts of it. Interested? Please contact us (myhits [at] sib.swiss).
Pagni M, Ioannidis V, Cerutti L, Zahn-Zabal M, Jongeneel CV, Hau J, Martin O, Kuznetsov D, Falquet L.
MyHits: improvements to an interactive resource for analyzing protein sequences.
Nucleic Acids Res. 2007 Jul; 35(Web Server issue):W433-7
- MyHits
| Description | RecName: Full=Probable ATP-dependent RNA helicase DDX23; EC=3.6.4.13; AltName: Full=100 kDa U5 snRNP-specific protein; AltName: Full=DEAD box protein 23; AltName: Full=PRP28 homolog; AltName: Full=U5-100kD; |
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| MyHits synonyms | DDX23_HUMAN , Q9BUQ8 , B2R600 , B4DH15 , O43188 , 01DD5BCF8BFBA2DB |
 Legends: 1, Phosphoserine. {ECO:0000244|PubMed:20068231, ECO:0000244|PubMed:21406692}; 2, Phosphoserine. {ECO:0000244|PubMed:20068231}; 3, Phosphoserine. {ECO:0000244|PubMed:21406692}; 4, CONFLICT P -> L (in Ref. 1; AAB87902). {ECO:0000305}; 5, CONFLICT D -> E (in Ref. 1; AAB87902). {ECO:0000305}; 6, CONFLICT L -> F (in Ref. 1; AAB87902). {ECO:0000305}; 7, Helicase ATP-binding. {ECO:0000255|PROSITE-ProRule:PRU00541}; 8, Helicase C-terminal. {ECO:0000255|PROSITE-ProRule:PRU00542}; 9, NP_BIND ATP. {ECO:0000255|PROSITE- ProRule:PRU00541}; 10, MOTIF Q motif; 11, MOTIF DEAD box; 12, COMPBIAS Arg-rich; 13, COMPBIAS Glu-rich; 14, VAR_SEQ SL -> RH (in isoform 2). {ECO:0000303|PubMed:14702039}; 15, ipfam:Helicase_C [T]; 16, ismart:HELICc [T]; 17, iprf:Q_MOTIF [T]; 18, iprf:HELICASE_CTER [T]; 19, ipat:DEAD_ATP_HELICASE [T]; 20, HELIX {ECO:0000244|PDB:4NHO}; 21, STRAND {ECO:0000244|PDB:4NHO}; 22, TURN {ECO:0000244|PDB:4NHO}.
| |
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 02-NOV-2016, entry version 150.
DE RecName: Full=Probable ATP-dependent RNA helicase DDX23;
DE EC=3.6.4.13;
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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-
RT containing, putative RNA helicase with significant homology to the
RT yeast splicing 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP SPLICEOSOMAL 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling 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
RT tri-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.,
RA Luehrmann R.;
RT "Phosphorylation of human PRP28 by SRPK2 is required for integration
RT of the 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
RT damage 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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation 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.,
RA Buerckstuemmer T., 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,
RP 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.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome 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.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Involved in pre-mRNA splicing and its phosphorylated
CC form (by SRPK2) is required for spliceosomal B complex formation.
CC {ECO:0000269|PubMed:18425142}.
CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate.
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
CC and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A,
CC WDR57, SNRNP40, DDX23, CD2BP2, PPIH, SNU13, EFTUD2, SART1 and
CC USP39. Identified in the spliceosome C complex. Interacts with
CC ERBB4. {ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:16723661,
CC ECO:0000269|PubMed:20858735, ECO:0000269|PubMed:9409622}.
CC -!- INTERACTION:
CC P54274:TERF1; NbExp=2; IntAct=EBI-540096, EBI-710997;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20858735,
CC ECO:0000269|PubMed:9409622}.
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 Note=No experimental confirmation available.;
CC -!- PTM: In vitro phosphorylated by CLK1 and U1 snRNP-associated
CC protein kinase. Phosphorylated by SRPK2 and this phosphorylation
CC is required for its association with the tri-snRNP (U4/U6-U5 tri-
CC small nuclear ribonucleoproteins) and subsequent spliceosomal B
CC complex formation. {ECO:0000269|PubMed:18425142,
CC ECO:0000269|PubMed:9409622}.
CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC subfamily. {ECO:0000305}.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00541}.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC {ECO:0000255|PROSITE-ProRule:PRU00542}.
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 UniGene; Hs.130098; -.
DR PDB; 3JCR; EM; 7.00 A; F=1-820.
DR PDB; 4NHO; X-ray; 2.00 A; A=338-820.
DR PDBsum; 3JCR; -.
DR PDBsum; 4NHO; -.
DR ProteinModelPortal; Q9BUQ8; -.
DR SMR; Q9BUQ8; -.
DR BioGrid; 114811; 80.
DR DIP; DIP-34974N; -.
DR IntAct; Q9BUQ8; 23.
DR MINT; MINT-1572793; -.
DR STRING; 9606.ENSP00000310723; -.
DR iPTMnet; Q9BUQ8; -.
DR PhosphoSitePlus; Q9BUQ8; -.
DR SwissPalm; Q9BUQ8; -.
DR BioMuta; DDX23; -.
DR DMDM; 160385708; -.
DR EPD; Q9BUQ8; -.
DR MaxQB; Q9BUQ8; -.
DR PaxDb; Q9BUQ8; -.
DR PeptideAtlas; Q9BUQ8; -.
DR PRIDE; Q9BUQ8; -.
DR DNASU; 9416; -.
DR Ensembl; ENST00000308025; ENSP00000310723; ENSG00000174243. [Q9BUQ8-1]
DR Ensembl; ENST00000547135; ENSP00000446770; ENSG00000174243. [Q9BUQ8-2]
DR GeneID; 9416; -.
DR KEGG; hsa:9416; -.
DR UCSC; uc001rsm.4; human. [Q9BUQ8-1]
DR CTD; 9416; -.
DR DisGeNET; 9416; -.
DR GeneCards; DDX23; -.
DR HGNC; HGNC:17347; DDX23.
DR HPA; HPA038680; -.
DR HPA; HPA039037; -.
DR MIM; 612172; gene.
DR neXtProt; NX_Q9BUQ8; -.
DR OpenTargets; ENSG00000174243; -.
DR PharmGKB; PA134934941; -.
DR eggNOG; KOG0333; Eukaryota.
DR eggNOG; ENOG410XNVG; LUCA.
DR GeneTree; ENSGT00820000127023; -.
DR HOGENOM; HOG000268796; -.
DR HOVERGEN; HBG102054; -.
DR InParanoid; Q9BUQ8; -.
DR KO; K12858; -.
DR OMA; NPIYKEK; -.
DR OrthoDB; EOG091G032I; -.
DR PhylomeDB; Q9BUQ8; -.
DR TreeFam; TF300527; -.
DR BioCyc; ZFISH:ENSG00000174243-MONOMER; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR ChiTaRS; DDX23; human.
DR GeneWiki; DDX23; -.
DR GenomeRNAi; 9416; -.
DR PRO; PR:Q9BUQ8; -.
DR Proteomes; UP000005640; Chromosome 12.
DR Bgee; ENSG00000174243; -.
DR CleanEx; HS_DDX23; -.
DR ExpressionAtlas; Q9BUQ8; baseline and differential.
DR Genevisible; Q9BUQ8; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:HPA.
DR GO; GO:0005682; C:U5 snRNP; IDA:HGNC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; TAS:ProtInc.
DR GO; GO:0044822; F:poly(A) RNA binding; IDA:UniProtKB.
DR GO; GO:0000354; P:cis assembly of pre-catalytic spliceosome; IC:HGNC.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR GO; GO:0000375; P:RNA splicing, via transesterification reactions; TAS:UniProtKB.
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; 2.
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; Complete proteome;
KW Direct protein sequencing; Helicase; Hydrolase; mRNA processing;
KW mRNA splicing; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome.
FT CHAIN 1 820 Probable ATP-dependent RNA helicase
FT DDX23.
FT /FTId=PRO_0000055128.
FT DOMAIN 422 627 Helicase ATP-binding.
FT {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT DOMAIN 651 799 Helicase C-terminal.
FT {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT NP_BIND 435 442 ATP. {ECO:0000255|PROSITE-
FT ProRule:PRU00541}.
FT MOTIF 391 419 Q motif.
FT MOTIF 549 552 DEAD box.
FT COMPBIAS 20 122 Arg-rich.
FT COMPBIAS 128 240 Glu-rich.
FT MOD_RES 14 14 Phosphoserine.
FT {ECO:0000244|PubMed:20068231,
FT ECO:0000244|PubMed:21406692}.
FT MOD_RES 16 16 Phosphoserine.
FT {ECO:0000244|PubMed:20068231}.
FT MOD_RES 107 107 Phosphoserine.
FT {ECO:0000244|PubMed:21406692}.
FT MOD_RES 109 109 Phosphoserine.
FT {ECO:0000244|PubMed:21406692}.
FT VAR_SEQ 107 108 SL -> RH (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_056575.
FT VAR_SEQ 109 820 Missing (in isoform 2).
FT {ECO:0000303|PubMed:14702039}.
FT /FTId=VSP_056576.
FT CONFLICT 137 137 P -> L (in Ref. 1; AAB87902).
FT {ECO:0000305}.
FT CONFLICT 281 281 D -> E (in Ref. 1; AAB87902).
FT {ECO:0000305}.
FT CONFLICT 309 309 L -> F (in Ref. 1; AAB87902).
FT {ECO:0000305}.
FT HELIX 357 359 {ECO:0000244|PDB:4NHO}.
FT HELIX 362 364 {ECO:0000244|PDB:4NHO}.
FT HELIX 367 377 {ECO:0000244|PDB:4NHO}.
FT STRAND 379 385 {ECO:0000244|PDB:4NHO}.
FT TURN 393 395 {ECO:0000244|PDB:4NHO}.
FT HELIX 400 409 {ECO:0000244|PDB:4NHO}.
FT HELIX 416 425 {ECO:0000244|PDB:4NHO}.
FT TURN 426 428 {ECO:0000244|PDB:4NHO}.
FT STRAND 431 434 {ECO:0000244|PDB:4NHO}.
FT HELIX 441 455 {ECO:0000244|PDB:4NHO}.
FT HELIX 458 461 {ECO:0000244|PDB:4NHO}.
FT STRAND 470 474 {ECO:0000244|PDB:4NHO}.
FT HELIX 478 492 {ECO:0000244|PDB:4NHO}.
FT HELIX 493 495 {ECO:0000244|PDB:4NHO}.
FT STRAND 499 502 {ECO:0000244|PDB:4NHO}.
FT STRAND 504 506 {ECO:0000244|PDB:4NHO}.
FT HELIX 508 516 {ECO:0000244|PDB:4NHO}.
FT STRAND 520 524 {ECO:0000244|PDB:4NHO}.
FT HELIX 526 534 {ECO:0000244|PDB:4NHO}.
FT STRAND 545 550 {ECO:0000244|PDB:4NHO}.
FT HELIX 551 556 {ECO:0000244|PDB:4NHO}.
FT HELIX 560 567 {ECO:0000244|PDB:4NHO}.
FT HELIX 572 574 {ECO:0000244|PDB:4NHO}.
FT HELIX 580 583 {ECO:0000244|PDB:4NHO}.
FT HELIX 585 593 {ECO:0000244|PDB:4NHO}.
FT HELIX 595 597 {ECO:0000244|PDB:4NHO}.
FT STRAND 601 607 {ECO:0000244|PDB:4NHO}.
FT HELIX 611 620 {ECO:0000244|PDB:4NHO}.
FT STRAND 625 629 {ECO:0000244|PDB:4NHO}.
FT HELIX 635 638 {ECO:0000244|PDB:4NHO}.
FT STRAND 639 645 {ECO:0000244|PDB:4NHO}.
FT HELIX 648 650 {ECO:0000244|PDB:4NHO}.
FT HELIX 651 660 {ECO:0000244|PDB:4NHO}.
FT STRAND 667 670 {ECO:0000244|PDB:4NHO}.
FT HELIX 674 686 {ECO:0000244|PDB:4NHO}.
FT STRAND 691 693 {ECO:0000244|PDB:4NHO}.
FT HELIX 704 712 {ECO:0000244|PDB:4NHO}.
FT STRAND 717 720 {ECO:0000244|PDB:4NHO}.
FT STRAND 734 740 {ECO:0000244|PDB:4NHO}.
FT HELIX 745 752 {ECO:0000244|PDB:4NHO}.
FT HELIX 753 755 {ECO:0000244|PDB:4NHO}.
FT STRAND 757 760 {ECO:0000244|PDB:4NHO}.
FT STRAND 763 768 {ECO:0000244|PDB:4NHO}.
FT HELIX 770 775 {ECO:0000244|PDB:4NHO}.
FT HELIX 776 784 {ECO:0000244|PDB:4NHO}.
FT HELIX 793 796 {ECO:0000244|PDB:4NHO}.
FT HELIX 799 801 {ECO:0000244|PDB:4NHO}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 651 759 ipfam:Helicase_C [T]
FT MYHIT 678 759 ismart:HELICc [T]
FT MYHIT 415 616 ipfam:DEAD [T]
FT MYHIT 410 642 ismart:DEXDc [T]
FT MYHIT 391 419 iprf:Q_MOTIF [T]
FT MYHIT 651 799 iprf:HELICASE_CTER [T]
FT MYHIT 422 627 iprf:HELICASE_ATP_BIND_1 [T]
FT MYHIT 547 555 ipat:DEAD_ATP_HELICASE [T]
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
//
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