ID   DDX23_HUMAN             Reviewed;         820 AA.
AC   Q9BUQ8; B2R600; O43188;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 3.
DT   03-NOV-2009, entry version 78.
DE   RecName: Full=Probable ATP-dependent RNA helicase DDX23;
DE            EC=3.6.1.-;
DE   AltName: Full=DEAD box protein 23;
DE   AltName: Full=100 kDa U5 snRNP-specific protein;
DE   AltName: Full=U5-100kD;
DE   AltName: Full=PRP28 homolog;
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], PROTEIN SEQUENCE OF 272-290; 409-419 AND
RP   433-441, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND IDENTIFICATION IN
RP   U5 AND U5/4/6 SNRNP COMPLEXES.
RX   MEDLINE=98072280; 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].
RC   TISSUE=Amygdala;
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].
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE
RP   SPICEOSOMAL 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   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RX   PubMed=16083285; DOI=10.1021/pr050048h;
RA   Kim J.-E., Tannenbaum S.R., White F.M.;
RT   "Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
RL   J. Proteome Res. 4:1339-1346(2005).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; THR-25; SER-107 AND
RP   SER-109, AND MASS SPECTROMETRY.
RC   TISSUE=Epithelium;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [9]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
CC   -!- FUNCTION: Probably involved in pre-mRNA splicing.
CC   -!- SUBUNIT: Component of the U5 and U5.4/6 snRNP complexes.
CC       Identified in the spliceosome C complex, at least composed of AQR,
CC       C19orf29, CDC40, CDC5L, CRNKL1, DDX23, DDX41, DDX48, DDX5, DGCR14,
CC       DHX35, DHX38, DHX8, EFTUD2, FRG1, GPATC1, HNRPA1, HNRPA2B1,
CC       HNRPA3, HNRPC, HNRPF, HNRPH1, HNRPK, HNRPM, HNRPR, HNRPU,
CC       KIAA1160, KIAA1604, LSM2, LSM3, MAGOH, MORG1, PABPC1, PLRG1, PNN,
CC       PPIE, PPIL1, PPIL3, PPWD1, PRPF19, PRPF4B, PRPF6, PRPF8, RALY,
CC       RBM22, RBM8A, RBMX, SART1, SF3A1, SF3A2, SF3A3, SF3B1, SF3B2,
CC       SF3B3, SFRS1, SKIV2L2, SNRNP200, SNRNP40, SNRPA1, SNRPB, SNRPB2,
CC       SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF, SNRPG, SNW1, SRRM1, SRRM2,
CC       SYF2, SYNCRIP, TFIP11, THOC4, U2AF1, XAB2 and ZCCHC8.
CC   -!- INTERACTION:
CC       O95400:CD2BP2; NbExp=1; IntAct=EBI-540096, EBI-768015;
CC       Q15287:RNPS1; NbExp=1; IntAct=EBI-540096, EBI-395959;
CC       Q96DI7:SNRNP40; NbExp=1; IntAct=EBI-540096, EBI-538492;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- PTM: In vitro phosphorylated by CLK1 and U1 snRNP-associated
CC       protein kinase.
CC   -!- SIMILARITY: Belongs to the DEAD box helicase family. DDX23/PRP28
CC       subfamily.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
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DR   EMBL; AF026402; AAB87902.1; -; mRNA.
DR   EMBL; AK312379; BAG35297.1; -; mRNA.
DR   EMBL; CH471111; EAW58011.1; -; Genomic_DNA.
DR   EMBL; BC002366; AAH02366.1; -; mRNA.
DR   IPI; IPI00006725; -.
DR   RefSeq; NP_004809.2; -.
DR   UniGene; Hs.130098; -.
DR   HSSP; Q58083; 1HV8.
DR   IntAct; Q9BUQ8; 4.
DR   STRING; Q9BUQ8; -.
DR   PhosphoSite; Q9BUQ8; -.
DR   PRIDE; Q9BUQ8; -.
DR   Ensembl; ENST00000308025; ENSP00000310723; ENSG00000174243; Homo sapiens.
DR   Ensembl; ENST00000398375; ENSP00000396892; ENSG00000174243; Homo sapiens.
DR   GeneID; 9416; -.
DR   KEGG; hsa:9416; -.
DR   UCSC; uc001rsm.1; human.
DR   CTD; 9416; -.
DR   GeneCards; GC12M047509; -.
DR   HGNC; HGNC:17347; DDX23.
DR   PharmGKB; PA134934941; -.
DR   HOGENOM; Q9BUQ8; -.
DR   HOVERGEN; Q9BUQ8; -.
DR   OMA; VQKILEY; -.
DR   Reactome; REACT_125; Processing of Capped Intron-Containing Pre-mRNA.
DR   Reactome; REACT_71; Gene Expression.
DR   NextBio; 35278; -.
DR   ArrayExpress; Q9BUQ8; -.
DR   Bgee; Q9BUQ8; -.
DR   CleanEx; HS_DDX23; -.
DR   Genevestigator; Q9BUQ8; -.
DR   GermOnline; ENSG00000174243; Homo sapiens.
DR   GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
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:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0031202; F:RNA splicing factor activity, transesterifi...; TAS:UniProtKB.
DR   GO; GO:0000354; P:cis assembly of pre-catalytic spliceosome; IC:HGNC.
DR   InterPro; IPR014001; DEAD-like_N.
DR   InterPro; IPR001650; DNA/RNA_helicase_C.
DR   InterPro; IPR011545; DNA/RNA_helicase_DEAD/DEAH_N.
DR   InterPro; IPR014021; Helicase_SF1/SF2_ATP-bd.
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   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   ATP-binding; Complete proteome; Direct protein sequencing; Helicase;
KW   Hydrolase; mRNA processing; mRNA splicing; Nucleotide-binding;
KW   Nucleus; Phosphoprotein; Spliceosome.
FT   CHAIN         1    820       Probable ATP-dependent RNA helicase
FT                                DDX23.
FT                                /FTId=PRO_0000055128.
FT   DOMAIN      422    627       Helicase ATP-binding.
FT   DOMAIN      651    799       Helicase C-terminal.
FT   NP_BIND     435    442       ATP (By similarity).
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   MOD_RES      25     25       Phosphothreonine.
FT   MOD_RES     107    107       Phosphoserine.
FT   MOD_RES     109    109       Phosphoserine.
FT   CONFLICT    137    137       P -> L (in Ref. 1; AAB87902).
FT   CONFLICT    281    281       D -> E (in Ref. 1; AAB87902).
FT   CONFLICT    309    309       L -> F (in Ref. 1; AAB87902).
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
//