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Q9BQ39

- DDX50_HUMAN

UniProt

Q9BQ39 - DDX50_HUMAN

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Protein

ATP-dependent RNA helicase DDX50

Gene

DDX50

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi181 – 1888ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX50 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 50
Gu-beta
Nucleolar protein Gu2
Gene namesi
Name:DDX50
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:17906. DDX50.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. membrane Source: UniProtKB
  2. nucleolus Source: HPA
  3. plasma membrane Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134948525.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 737737ATP-dependent RNA helicase DDX50PRO_0000055054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei41 – 411Phosphoserine1 Publication
Modified residuei82 – 821Phosphoserine2 Publications
Modified residuei86 – 861Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9BQ39.
PaxDbiQ9BQ39.
PeptideAtlasiQ9BQ39.
PRIDEiQ9BQ39.

2D gel databases

SWISS-2DPAGEQ9BQ39.

PTM databases

PhosphoSiteiQ9BQ39.

Expressioni

Gene expression databases

BgeeiQ9BQ39.
CleanExiHS_DDX50.
ExpressionAtlasiQ9BQ39. baseline.
GenevestigatoriQ9BQ39.

Organism-specific databases

HPAiHPA037388.

Interactioni

Subunit structurei

Interacts with C1QBP.1 Publication

Protein-protein interaction databases

BioGridi122480. 20 interactions.
IntActiQ9BQ39. 9 interactions.
MINTiMINT-4727989.
STRINGi9606.ENSP00000362687.

Structurei

Secondary structure

1
737
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi587 – 5937
Helixi602 – 61110
Helixi614 – 6174
Beta strandi621 – 6255
Beta strandi629 – 6379
Helixi638 – 64710
Beta strandi650 – 6523
Beta strandi654 – 6563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E29NMR-A575-659[»]
ProteinModelPortaliQ9BQ39.
SMRiQ9BQ39. Positions 123-659.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BQ39.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini168 – 347180Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini380 – 524145Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi137 – 16529Q motifAdd
BLAST
Motifi290 – 2934DEVD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi677 – 72852Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 helicase ATP-binding domain.PROSITE-ProRule annotation
Contains 1 helicase C-terminal domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00760000119219.
HOGENOMiHOG000268805.
HOVERGENiHBG051331.
InParanoidiQ9BQ39.
KOiK13183.
OMAiNSHKSSD.
OrthoDBiEOG77HDD6.
PhylomeDBiQ9BQ39.
TreeFamiTF328622.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR012562. GUCT.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF08152. GUCT. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9BQ39 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MPGKLLWGDI MELEAPLEES ESQKKERQKS DRRKSRHHYD SDEKSETREN
60 70 80 90 100
GVTDDLDAPK AKKSKMKEKL NGDTEEGFNR LSDEFSKSHK SRRKDLPNGD
110 120 130 140 150
IDEYEKKSKR VSSLDTSTHK SSDNKLEETL TREQKEGAFS NFPISEETIK
160 170 180 190 200
LLKGRGVTYL FPIQVKTFGP VYEGKDLIAQ ARTGTGKTFS FAIPLIERLQ
210 220 230 240 250
RNQETIKKSR SPKVLVLAPT RELANQVAKD FKDITRKLSV ACFYGGTSYQ
260 270 280 290 300
SQINHIRNGI DILVGTPGRI KDHLQSGRLD LSKLRHVVLD EVDQMLDLGF
310 320 330 340 350
AEQVEDIIHE SYKTDSEDNP QTLLFSATCP QWVYKVAKKY MKSRYEQVDL
360 370 380 390 400
VGKMTQKAAT TVEHLAIQCH WSQRPAVIGD VLQVYSGSEG RAIIFCETKK
410 420 430 440 450
NVTEMAMNPH IKQNAQCLHG DIAQSQREIT LKGFREGSFK VLVATNVAAR
460 470 480 490 500
GLDIPEVDLV IQSSPPQDVE SYIHRSGRTG RAGRTGICIC FYQPRERGQL
510 520 530 540 550
RYVEQKAGIT FKRVGVPSTM DLVKSKSMDA IRSLASVSYA AVDFFRPSAQ
560 570 580 590 600
RLIEEKGAVD ALAAALAHIS GASSFEPRSL ITSDKGFVTM TLESLEEIQD
610 620 630 640 650
VSCAWKELNR KLSSNAVSQI TRMCLLKGNM GVCFDVPTTE SERLQAEWHD
660 670 680 690 700
SDWILSVPAK LPEIEEYYDG NTSSNSRQRS GWSSGRSGRS GRSGGRSGGR
710 720 730
SGRQSRQGSR SGSRQDGRRR SGNRNRSRSG GHKRSFD
Length:737
Mass (Da):82,565
Last modified:June 1, 2001 - v1
Checksum:i9B7EF72EEC7C504E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti680 – 6801S → I in AAH18637. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF334103 mRNA. Translation: AAK29402.1.
AL359844 Genomic DNA. Translation: CAH72376.1.
CH471083 Genomic DNA. Translation: EAW54304.1.
BC000210 mRNA. Translation: AAH00210.1.
BC000272 mRNA. Translation: AAH00272.1.
BC018637 mRNA. Translation: AAH18637.2.
CCDSiCCDS7283.1.
RefSeqiNP_076950.1. NM_024045.1.
UniGeneiHs.522984.

Genome annotation databases

EnsembliENST00000373585; ENSP00000362687; ENSG00000107625.
GeneIDi79009.
KEGGihsa:79009.
UCSCiuc001jou.3. human.

Polymorphism databases

DMDMi55976580.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF334103 mRNA. Translation: AAK29402.1 .
AL359844 Genomic DNA. Translation: CAH72376.1 .
CH471083 Genomic DNA. Translation: EAW54304.1 .
BC000210 mRNA. Translation: AAH00210.1 .
BC000272 mRNA. Translation: AAH00272.1 .
BC018637 mRNA. Translation: AAH18637.2 .
CCDSi CCDS7283.1.
RefSeqi NP_076950.1. NM_024045.1.
UniGenei Hs.522984.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E29 NMR - A 575-659 [» ]
ProteinModelPortali Q9BQ39.
SMRi Q9BQ39. Positions 123-659.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 122480. 20 interactions.
IntActi Q9BQ39. 9 interactions.
MINTi MINT-4727989.
STRINGi 9606.ENSP00000362687.

PTM databases

PhosphoSitei Q9BQ39.

Polymorphism databases

DMDMi 55976580.

2D gel databases

SWISS-2DPAGE Q9BQ39.

Proteomic databases

MaxQBi Q9BQ39.
PaxDbi Q9BQ39.
PeptideAtlasi Q9BQ39.
PRIDEi Q9BQ39.

Protocols and materials databases

DNASUi 79009.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373585 ; ENSP00000362687 ; ENSG00000107625 .
GeneIDi 79009.
KEGGi hsa:79009.
UCSCi uc001jou.3. human.

Organism-specific databases

CTDi 79009.
GeneCardsi GC10P070661.
HGNCi HGNC:17906. DDX50.
HPAi HPA037388.
MIMi 610373. gene.
neXtProti NX_Q9BQ39.
PharmGKBi PA134948525.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00760000119219.
HOGENOMi HOG000268805.
HOVERGENi HBG051331.
InParanoidi Q9BQ39.
KOi K13183.
OMAi NSHKSSD.
OrthoDBi EOG77HDD6.
PhylomeDBi Q9BQ39.
TreeFami TF328622.

Miscellaneous databases

ChiTaRSi DDX50. human.
EvolutionaryTracei Q9BQ39.
GeneWikii DDX50.
GenomeRNAii 79009.
NextBioi 67657.
PROi Q9BQ39.
SOURCEi Search...

Gene expression databases

Bgeei Q9BQ39.
CleanExi HS_DDX50.
ExpressionAtlasi Q9BQ39. baseline.
Genevestigatori Q9BQ39.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
IPR012562. GUCT.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF08152. GUCT. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi 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. "Genomic structure of newly identified paralogue of RNA helicase II/Gu: detection of pseudogenes and multiple alternatively spliced mRNAs."
    Valdez B.C., Yang H., Hong E., Sequitin A.M.
    Gene 284:53-61(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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: Eye and Skin.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "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-82 AND SER-86, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
    Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
    Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  10. "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-41, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Solution structure of the GUCT domain from human RNA helicase II/Gu beta reveals the RRM fold, but implausible RNA interactions."
    Ohnishi S., Paakkonen K., Koshiba S., Tochio N., Sato M., Kobayashi N., Harada T., Watanabe S., Muto Y., Guntert P., Tanaka A., Kigawa T., Yokoyama S.
    Proteins 74:133-144(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 570-659.

Entry informationi

Entry nameiDDX50_HUMAN
AccessioniPrimary (citable) accession number: Q9BQ39
Secondary accession number(s): Q5VX37, Q8WV76, Q9BWI8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 23, 2004
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 122 of the entry and version 1 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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