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Q9BUQ8 (DDX23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable ATP-dependent RNA helicase DDX23

EC=3.6.4.13
Alternative name(s):
100 kDa U5 snRNP-specific protein
DEAD box protein 23
PRP28 homolog
U5-100kD
Gene names
Name:DDX23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length820 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation. Ref.8

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

The phosphorylated form (by SRPK2) is a component of the U4/U6-U5 tri-snRNP complex composed of the U4, U6 and U5 snRNAs and at least PRPF3, PRPF4, PRPF6, PRPF8, PRPF31, SNRNP200, TXNL4A, WDR57, SNRNP40, DDX23, CD2BP2, PPIH, NHP2L1, EFTUD2, SART1 and USP39. Identified in the spliceosome C complex. Interacts with ERBB4. Ref.1 Ref.5 Ref.7 Ref.9

Subcellular location

Nucleus Ref.1 Ref.9.

Post-translational modification

In vitro phosphorylated by CLK1 and U1 snRNP-associated protein kinase. Phosphorylated by SRPK2 and this phosphorylation is required for its association with the tri-snRNP (U4/U6-U5 tri-small nuclear ribonucleoproteins) and subsequent spliceosomal B complex formation. Ref.1 Ref.8

Sequence similarities

Belongs to the DEAD box helicase family. DDX23/PRP28 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Biological processmRNA processing
mRNA splicing
   Cellular componentNucleus
Spliceosome
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processATP catabolic process

Traceable author statement Ref.1. Source: GOC

RNA splicing

Traceable author statement. Source: Reactome

RNA splicing, via transesterification reactions

Traceable author statement Ref.1. Source: UniProtKB

cis assembly of pre-catalytic spliceosome

Inferred by curator PubMed 9539711. Source: HGNC

gene expression

Traceable author statement. Source: Reactome

mRNA splicing, via spliceosome

Inferred by curator Ref.5. Source: UniProtKB

   Cellular_componentU5 snRNP

Inferred from direct assay PubMed 9539711. Source: HGNC

catalytic step 2 spliceosome

Inferred from direct assay Ref.5. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708. Source: UniProt

mitochondrion

Inferred from direct assay. Source: HPA

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay. Source: HPA

plasma membrane

Inferred from direct assay. Source: HPA

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent RNA helicase activity

Traceable author statement Ref.1. Source: ProtInc

poly(A) RNA binding

Inferred from direct assay PubMed 22681889. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 820820Probable ATP-dependent RNA helicase DDX23
PRO_0000055128

Regions

Domain422 – 627206Helicase ATP-binding
Domain651 – 799149Helicase C-terminal
Nucleotide binding435 – 4428ATP By similarity
Motif391 – 41929Q motif
Motif549 – 5524DEAD box
Compositional bias20 – 122103Arg-rich
Compositional bias128 – 240113Glu-rich

Amino acid modifications

Modified residue141Phosphoserine Ref.10 Ref.12
Modified residue161Phosphoserine Ref.10
Modified residue1071Phosphoserine Ref.12
Modified residue1091Phosphoserine Ref.12

Experimental info

Sequence conflict1371P → L in AAB87902. Ref.1
Sequence conflict2811D → E in AAB87902. Ref.1
Sequence conflict3091L → F in AAB87902. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9BUQ8 [UniParc].

Last modified October 23, 2007. Version 3.
Checksum: 01DD5BCF8BFBA2DB

FASTA82095,583
        10         20         30         40         50         60 
MAGELADKKD RDASPSKEER KRSRTPDRER DRDRDRKSSP SKDRKRHRSR DRRRGGSRSR 

        70         80         90        100        110        120 
SRSRSKSAER ERRHKERERD KERDRNKKDR DRDKDGHRRD KDRKRSSLSP GRGKDFKSRK 

       130        140        150        160        170        180 
DRDSKKDEED EHGDKKPKAQ PLSLEELLAK KKAEEEAEAK PKFLSKAERE AEALKRRQQE 

       190        200        210        220        230        240 
VEERQRMLEE ERKKRKQFQD LGRKMLEDPQ ERERRERRER MERETNGNED EEGRQKIREE 

       250        260        270        280        290        300 
KDKSKELHAI KERYLGGIKK RRRTRHLNDR KFVFEWDASE DTSIDYNPLY KERHQVQLLG 

       310        320        330        340        350        360 
RGFIAGIDLK QQKREQSRFY GDLMEKRRTL EEKEQEEARL RKLRKKEAKQ RWDDRHWSQK 

       370        380        390        400        410        420 
KLDEMTDRDW RIFREDYSIT TKGGKIPNPI RSWKDSSLPP HILEVIDKCG YKEPTPIQRQ 

       430        440        450        460        470        480 
AIPIGLQNRD IIGVAETGSG KTAAFLIPLL VWITTLPKID RIEESDQGPY AIILAPTREL 

       490        500        510        520        530        540 
AQQIEEETIK FGKPLGIRTV AVIGGISRED QGFRLRMGCE IVIATPGRLI DVLENRYLVL 

       550        560        570        580        590        600 
SRCTYVVLDE ADRMIDMGFE PDVQKILEHM PVSNQKPDTD EAEDPEKMLA NFESGKHKYR 

       610        620        630        640        650        660 
QTVMFTATMP PAVERLARSY LRRPAVVYIG SAGKPHERVE QKVFLMSESE KRKKLLAILE 

       670        680        690        700        710        720 
QGFDPPIIIF VNQKKGCDVL AKSLEKMGYN ACTLHGGKGQ EQREFALSNL KAGAKDILVA 

       730        740        750        760        770        780 
TDVAGRGIDI QDVSMVVNYD MAKNIEDYIH RIGRTGRAGK SGVAITFLTK EDSAVFYELK 

       790        800        810        820 
QAILESPVSS CPPELANHPD AQHKPGTILT KKRREETIFA 

« Hide

References

« Hide 'large scale' references
[1]"The human U5 snRNP-specific 100-kD protein is an RS domain-containing, putative RNA helicase with significant homology to the yeast splicing factor Prp28p."
Teigelkamp S., Mundt C., Achsel T., Will C.L., Luehrmann R.
RNA 3:1313-1326(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 272-290; 409-419 AND 433-441, SUBCELLULAR LOCATION, PHOSPHORYLATION, IDENTIFICATION IN U5 AND U5/4/6 SNRNP COMPLEXES.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala.
[3]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[5]"Purification and characterization of native spliceosomes suitable for three-dimensional structural analysis."
Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.
RNA 8:426-439(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE SPLICEOSOMAL C COMPLEX.
[6]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[7]"The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP."
Liu S., Rauhut R., Vornlocher H.-P., Luehrmann R.
RNA 12:1418-1430(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBUNIT.
[8]"Phosphorylation of human PRP28 by SRPK2 is required for integration of the U4/U6-U5 tri-snRNP into the spliceosome."
Mathew R., Hartmuth K., Moehlmann S., Urlaub H., Ficner R., Luehrmann R.
Nat. Struct. Mol. Biol. 15:435-443(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION BY SRPK2.
[9]"Interactions of ErbB4 and Kap1 connect the growth factor and DNA damage response pathways."
Gilmore-Hebert M., Ramabhadran R., Stern D.F.
Mol. Cancer Res. 8:1388-1398(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH ERBB4, SUBCELLULAR LOCATION.
[10]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14 AND SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14; SER-107 AND SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026402 mRNA. Translation: AAB87902.1.
AK312379 mRNA. Translation: BAG35297.1.
CH471111 Genomic DNA. Translation: EAW58011.1.
BC002366 mRNA. Translation: AAH02366.1.
RefSeqNP_004809.2. NM_004818.2.
UniGeneHs.130098.

3D structure databases

ProteinModelPortalQ9BUQ8.
SMRQ9BUQ8. Positions 351-795.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114811. 29 interactions.
DIPDIP-34974N.
IntActQ9BUQ8. 9 interactions.
MINTMINT-1572793.
STRING9606.ENSP00000310723.

PTM databases

PhosphoSiteQ9BUQ8.

Polymorphism databases

DMDM160385708.

Proteomic databases

PaxDbQ9BUQ8.
PRIDEQ9BUQ8.

Protocols and materials databases

DNASU9416.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308025; ENSP00000310723; ENSG00000174243.
GeneID9416.
KEGGhsa:9416.
UCSCuc001rsm.3. human.

Organism-specific databases

CTD9416.
GeneCardsGC12M049223.
HGNCHGNC:17347. DDX23.
HPAHPA038680.
MIM612172. gene.
neXtProtNX_Q9BUQ8.
PharmGKBPA134934941.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268796.
HOVERGENHBG102054.
InParanoidQ9BUQ8.
KOK12858.
OMAPIRNWKE.
OrthoDBEOG7XH6P9.
PhylomeDBQ9BUQ8.
TreeFamTF300527.

Enzyme and pathway databases

ReactomeREACT_71. Gene Expression.

Gene expression databases

ArrayExpressQ9BUQ8.
BgeeQ9BUQ8.
CleanExHS_DDX23.
GenevestigatorQ9BUQ8.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR000629. RNA-helicase_DEAD-box_CS.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 2 hits.
PROSITEPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiDDX23.
GenomeRNAi9416.
NextBio35278.
PROQ9BUQ8.
SOURCESearch...

Entry information

Entry nameDDX23_HUMAN
AccessionPrimary (citable) accession number: Q9BUQ8
Secondary accession number(s): B2R600, O43188
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 23, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM