Q9BUQ8 (DDX23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	820 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	mRNA processing mRNA splicing
Cellular component	Nucleus Spliceosome
Ligand	ATP-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cis assembly of pre-catalytic spliceosome Inferred by curator PubMed 9539711. Source: HGNC
Cellular_component	U5 snRNP Inferred from direct assay PubMed 9539711. Source: HGNC catalytic step 2 spliceosome Inferred from direct assay Ref.5. Source: UniProtKB mitochondrion Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Traceable author statement Ref.1. Source: ProtInc nucleic acid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 820	820	Probable ATP-dependent RNA helicase DDX23		PRO_0000055128
Regions
	Domain	422 – 627	206	Helicase ATP-binding
	Domain	651 – 799	149	Helicase C-terminal
	Nucleotide binding	435 – 442	8	ATP By similarity
	Motif	391 – 419	29	Q motif
	Motif	549 – 552	4	DEAD box
	Compositional bias	20 – 122	103	Arg-rich
	Compositional bias	128 – 240	113	Glu-rich
Amino acid modifications
	Modified residue	14	1	Phosphoserine Ref.10 Ref.12
	Modified residue	16	1	Phosphoserine Ref.10
	Modified residue	107	1	Phosphoserine Ref.12
	Modified residue	109	1	Phosphoserine Ref.12
Experimental info
	Sequence conflict	137	1	P → L in AAB87902. Ref.1
	Sequence conflict	281	1	D → E in AAB87902. Ref.1
	Sequence conflict	309	1	L → F in AAB87902. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q9BUQ8 [UniParc]. Last modified October 23, 2007. Version 3. Checksum: 01DD5BCF8BFBA2DB	FASTA	820	95,583
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00006725.
RefSeq	NP_004809.2. NM_004818.2.
UniGene	Hs.130098.
3D structure databases
ProteinModelPortal	Q9BUQ8.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-34974N.
IntAct	Q9BUQ8. 7 interactions.
MINT	MINT-1572793.
STRING	9606.ENSP00000310723.
PTM databases
PhosphoSite	Q9BUQ8.
Polymorphism databases
DMDM	160385708.
Proteomic databases
PaxDb	Q9BUQ8.
PRIDE	Q9BUQ8.
Protocols and materials databases
DNASU	9416.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308025; ENSP00000310723; ENSG00000174243.
GeneID	9416.
KEGG	hsa:9416.
UCSC	uc001rsm.3. human.
Organism-specific databases
CTD	9416.
GeneCards	GC12M049223.
HGNC	HGNC:17347. DDX23.
HPA	HPA038680.
MIM	612172. gene.
neXtProt	NX_Q9BUQ8.
PharmGKB	PA134934941.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0513.
HOGENOM	HOG000268796.
HOVERGEN	HBG102054.
InParanoid	Q9BUQ8.
KO	K12858.
OMA	PIRNWKE.
OrthoDB	EOG46T312.
PhylomeDB	Q9BUQ8.
Enzyme and pathway databases
Reactome	REACT_1675. mRNA Processing. REACT_71. Gene Expression.
Gene expression databases
ArrayExpress	Q9BUQ8.
Bgee	Q9BUQ8.
CleanEx	HS_DDX23.
Genevestigator	Q9BUQ8.
GermOnline	ENSG00000174243. Homo sapiens.
Family and domain databases
InterPro	IPR011545. DNA/RNA_helicase_DEAD/DEAH_N. IPR014001. Helicase_ATP-bd. IPR001650. Helicase_C. IPR000629. RNA-helicase_DEAD-box_CS. IPR014014. RNA_helicase_DEAD_Q_motif. [Graphical view]
Pfam	PF00270. DEAD. 1 hit. PF00271. Helicase_C. 1 hit. [Graphical view]
SMART	SM00487. DEXDc. 1 hit. SM00490. HELICc. 1 hit. [Graphical view]
PROSITE	PS00039. DEAD_ATP_HELICASE. 1 hit. PS51192. HELICASE_ATP_BIND_1. 1 hit. PS51194. HELICASE_CTER. 1 hit. PS51195. Q_MOTIF. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9416.
NextBio	35278.
SOURCE	Search...

Entry information

Entry name

DDX23_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 113 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.