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Q9BUQ8

- DDX23_HUMAN

UniProt

Q9BUQ8 - DDX23_HUMAN

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Protein
Probable ATP-dependent RNA helicase DDX23
Gene
DDX23
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in pre-mRNA splicing and its phosphorylated form (by SRPK2) is required for spliceosomal B complex formation.1 Publication

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi435 – 4428ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: ProtInc
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. ATP catabolic process Source: GOC
  2. RNA splicing Source: Reactome
  3. RNA splicing, via transesterification reactions Source: UniProtKB
  4. cis assembly of pre-catalytic spliceosome Source: HGNC
  5. gene expression Source: Reactome
  6. mRNA splicing, via spliceosome Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Names & Taxonomyi

Protein namesi
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 namesi
Name:DDX23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17347. DDX23.

Subcellular locationi

Nucleus 2 Publications

GO - Cellular componenti

  1. U5 snRNP Source: HGNC
  2. catalytic step 2 spliceosome Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProt
  4. mitochondrion Source: HPA
  5. nucleoplasm Source: Reactome
  6. nucleus Source: HPA
  7. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus, Spliceosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134934941.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 820820Probable ATP-dependent RNA helicase DDX23
PRO_0000055128Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei14 – 141Phosphoserine2 Publications
Modified residuei16 – 161Phosphoserine1 Publication
Modified residuei107 – 1071Phosphoserine1 Publication
Modified residuei109 – 1091Phosphoserine1 Publication

Post-translational modificationi

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.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BUQ8.
PaxDbiQ9BUQ8.
PRIDEiQ9BUQ8.

PTM databases

PhosphoSiteiQ9BUQ8.

Expressioni

Gene expression databases

ArrayExpressiQ9BUQ8.
BgeeiQ9BUQ8.
CleanExiHS_DDX23.
GenevestigatoriQ9BUQ8.

Organism-specific databases

HPAiHPA038680.

Interactioni

Subunit structurei

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 ERBB4.4 Publications

Protein-protein interaction databases

BioGridi114811. 34 interactions.
DIPiDIP-34974N.
IntActiQ9BUQ8. 9 interactions.
MINTiMINT-1572793.
STRINGi9606.ENSP00000310723.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4NHOX-ray2.00A338-820[»]
ProteinModelPortaliQ9BUQ8.
SMRiQ9BUQ8. Positions 350-795.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini422 – 627206Helicase ATP-binding
Add
BLAST
Domaini651 – 799149Helicase C-terminal
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi391 – 41929Q motif
Add
BLAST
Motifi549 – 5524DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 122103Arg-rich
Add
BLAST
Compositional biasi128 – 240113Glu-rich
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0513.
HOGENOMiHOG000268796.
HOVERGENiHBG102054.
InParanoidiQ9BUQ8.
KOiK12858.
OMAiPIRNWKE.
OrthoDBiEOG7XH6P9.
PhylomeDBiQ9BUQ8.
TreeFamiTF300527.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. 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]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 2 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BUQ8-1 [UniParc]FASTAAdd to Basket

« Hide

MAGELADKKD RDASPSKEER KRSRTPDRER DRDRDRKSSP SKDRKRHRSR    50
DRRRGGSRSR SRSRSKSAER ERRHKERERD KERDRNKKDR DRDKDGHRRD 100
KDRKRSSLSP GRGKDFKSRK DRDSKKDEED EHGDKKPKAQ PLSLEELLAK 150
KKAEEEAEAK PKFLSKAERE AEALKRRQQE VEERQRMLEE ERKKRKQFQD 200
LGRKMLEDPQ ERERRERRER MERETNGNED EEGRQKIREE KDKSKELHAI 250
KERYLGGIKK RRRTRHLNDR KFVFEWDASE DTSIDYNPLY KERHQVQLLG 300
RGFIAGIDLK QQKREQSRFY GDLMEKRRTL EEKEQEEARL RKLRKKEAKQ 350
RWDDRHWSQK KLDEMTDRDW RIFREDYSIT TKGGKIPNPI RSWKDSSLPP 400
HILEVIDKCG YKEPTPIQRQ AIPIGLQNRD IIGVAETGSG KTAAFLIPLL 450
VWITTLPKID RIEESDQGPY AIILAPTREL AQQIEEETIK FGKPLGIRTV 500
AVIGGISRED QGFRLRMGCE IVIATPGRLI DVLENRYLVL SRCTYVVLDE 550
ADRMIDMGFE PDVQKILEHM PVSNQKPDTD EAEDPEKMLA NFESGKHKYR 600
QTVMFTATMP PAVERLARSY LRRPAVVYIG SAGKPHERVE QKVFLMSESE 650
KRKKLLAILE QGFDPPIIIF VNQKKGCDVL AKSLEKMGYN ACTLHGGKGQ 700
EQREFALSNL KAGAKDILVA TDVAGRGIDI QDVSMVVNYD MAKNIEDYIH 750
RIGRTGRAGK SGVAITFLTK EDSAVFYELK QAILESPVSS CPPELANHPD 800
AQHKPGTILT KKRREETIFA 820
Length:820
Mass (Da):95,583
Last modified:October 23, 2007 - v3
Checksum:i01DD5BCF8BFBA2DB
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371P → L in AAB87902. 1 Publication
Sequence conflicti281 – 2811D → E in AAB87902. 1 Publication
Sequence conflicti309 – 3091L → F in AAB87902. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026402 mRNA. Translation: AAB87902.1.
AK312379 mRNA. Translation: BAG35297.1.
CH471111 Genomic DNA. Translation: EAW58011.1.
BC002366 mRNA. Translation: AAH02366.1.
CCDSiCCDS8770.1.
RefSeqiNP_004809.2. NM_004818.2.
UniGeneiHs.130098.

Genome annotation databases

EnsembliENST00000308025; ENSP00000310723; ENSG00000174243.
GeneIDi9416.
KEGGihsa:9416.
UCSCiuc001rsm.3. human.

Polymorphism databases

DMDMi160385708.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF026402 mRNA. Translation: AAB87902.1 .
AK312379 mRNA. Translation: BAG35297.1 .
CH471111 Genomic DNA. Translation: EAW58011.1 .
BC002366 mRNA. Translation: AAH02366.1 .
CCDSi CCDS8770.1.
RefSeqi NP_004809.2. NM_004818.2.
UniGenei Hs.130098.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4NHO X-ray 2.00 A 338-820 [» ]
ProteinModelPortali Q9BUQ8.
SMRi Q9BUQ8. Positions 350-795.
ModBasei Search...

Protein-protein interaction databases

BioGridi 114811. 34 interactions.
DIPi DIP-34974N.
IntActi Q9BUQ8. 9 interactions.
MINTi MINT-1572793.
STRINGi 9606.ENSP00000310723.

PTM databases

PhosphoSitei Q9BUQ8.

Polymorphism databases

DMDMi 160385708.

Proteomic databases

MaxQBi Q9BUQ8.
PaxDbi Q9BUQ8.
PRIDEi Q9BUQ8.

Protocols and materials databases

DNASUi 9416.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000308025 ; ENSP00000310723 ; ENSG00000174243 .
GeneIDi 9416.
KEGGi hsa:9416.
UCSCi uc001rsm.3. human.

Organism-specific databases

CTDi 9416.
GeneCardsi GC12M049223.
HGNCi HGNC:17347. DDX23.
HPAi HPA038680.
MIMi 612172. gene.
neXtProti NX_Q9BUQ8.
PharmGKBi PA134934941.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
HOGENOMi HOG000268796.
HOVERGENi HBG102054.
InParanoidi Q9BUQ8.
KOi K12858.
OMAi PIRNWKE.
OrthoDBi EOG7XH6P9.
PhylomeDBi Q9BUQ8.
TreeFami TF300527.

Enzyme and pathway databases

Reactomei REACT_1753. mRNA Splicing - Minor Pathway.
REACT_467. mRNA Splicing - Major Pathway.

Miscellaneous databases

GeneWikii DDX23.
GenomeRNAii 9416.
NextBioi 35278.
PROi Q9BUQ8.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9BUQ8.
Bgeei Q9BUQ8.
CleanExi HS_DDX23.
Genevestigatori Q9BUQ8.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. 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 ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 2 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiDDX23_HUMAN
AccessioniPrimary (citable) accession number: Q9BUQ8
Secondary accession number(s): B2R600, O43188
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: October 23, 2007
Last modified: September 3, 2014
This is version 126 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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