Q9BQ39 (DDX50_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

DDX50

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	737 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	Interacts with C1QBP. Ref.9
Subcellular location	Nucleus › nucleolus Ref.5.
Sequence similarities	Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.

Ontologies

Keywords
Cellular component	Nucleus
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	nucleolus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent helicase activity Inferred from electronic annotation. Source: InterPro RNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 737

737

ATP-dependent RNA helicase DDX50

PRO_0000055054

Regions

Domain

168 – 347

180

Helicase ATP-binding

Domain

380 – 524

145

Helicase C-terminal

Nucleotide binding

181 – 188

8

ATP By similarity

Motif

137 – 165

29

Q motif

Motif

290 – 293

4

DEVD box

Compositional bias

677 – 728

52

Arg-rich

Amino acid modifications

Modified residue

41

1

Phosphoserine Ref.10

Modified residue

82

1

Phosphoserine Ref.6 Ref.7

Modified residue

86

1

Phosphoserine Ref.7

Experimental info

Sequence conflict

680

1

S → I in AAH18637. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

737

Helix Strand Turn

Details...

Beta strand

587 – 593

7

Helix

602 – 611

10

Helix

614 – 617

4

Beta strand

621 – 625

5

Beta strand

629 – 637

9

Helix

638 – 647

10

Beta strand

650 – 652

3

Beta strand

654 – 656

3

Sequences

	Sequence		Length	Mass (Da)
	Q9BQ39 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 9B7EF72EEC7C504E	FASTA	737	82,565
	10 20 30 40 50 60 MPGKLLWGDI MELEAPLEES ESQKKERQKS DRRKSRHHYD SDEKSETREN GVTDDLDAPK 70 80 90 100 110 120 AKKSKMKEKL NGDTEEGFNR LSDEFSKSHK SRRKDLPNGD IDEYEKKSKR VSSLDTSTHK 130 140 150 160 170 180 SSDNKLEETL TREQKEGAFS NFPISEETIK LLKGRGVTYL FPIQVKTFGP VYEGKDLIAQ 190 200 210 220 230 240 ARTGTGKTFS FAIPLIERLQ RNQETIKKSR SPKVLVLAPT RELANQVAKD FKDITRKLSV 250 260 270 280 290 300 ACFYGGTSYQ SQINHIRNGI DILVGTPGRI KDHLQSGRLD LSKLRHVVLD EVDQMLDLGF 310 320 330 340 350 360 AEQVEDIIHE SYKTDSEDNP QTLLFSATCP QWVYKVAKKY MKSRYEQVDL VGKMTQKAAT 370 380 390 400 410 420 TVEHLAIQCH WSQRPAVIGD VLQVYSGSEG RAIIFCETKK NVTEMAMNPH IKQNAQCLHG 430 440 450 460 470 480 DIAQSQREIT LKGFREGSFK VLVATNVAAR GLDIPEVDLV IQSSPPQDVE SYIHRSGRTG 490 500 510 520 530 540 RAGRTGICIC FYQPRERGQL RYVEQKAGIT FKRVGVPSTM DLVKSKSMDA IRSLASVSYA 550 560 570 580 590 600 AVDFFRPSAQ RLIEEKGAVD ALAAALAHIS GASSFEPRSL ITSDKGFVTM TLESLEEIQD 610 620 630 640 650 660 VSCAWKELNR KLSSNAVSQI TRMCLLKGNM GVCFDVPTTE SERLQAEWHD SDWILSVPAK 670 680 690 700 710 720 LPEIEEYYDG NTSSNSRQRS GWSSGRSGRS GRSGGRSGGR SGRQSRQGSR SGSRQDGRRR 730 SGNRNRSRSG GHKRSFD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	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: Eye and Skin.
[5]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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].
[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, MASS SPECTROMETRY.
[11]	"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00031554.

RefSeq

NP_076950.1. NM_024045.1.

UniGene

Hs.522984.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2E29	NMR	-	A	570-659	[»]

ProteinModelPortal

Q9BQ39.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BQ39. 7 interactions.

MINT

MINT-4727989.

STRING

9606.ENSP00000362687.

PTM databases

PhosphoSite

Q9BQ39.

Polymorphism databases

DMDM

55976580.

2D gel databases

SWISS-2DPAGE

Q9BQ39.

Proteomic databases

PaxDb

Q9BQ39.

PeptideAtlas

Q9BQ39.

PRIDE

Q9BQ39.

Protocols and materials databases

DNASU

79009.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000373585; ENSP00000362687; ENSG00000107625.

GeneID

79009.

KEGG

hsa:79009.

UCSC

uc001jou.3. human.

Organism-specific databases

CTD

79009.

GeneCards

GC10P070661.

HGNC

HGNC:17906. DDX50.

HPA

HPA037388.

MIM

610373. gene.

neXtProt

NX_Q9BQ39.

PharmGKB

PA134948525.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268805.

HOVERGEN

HBG051331.

InParanoid

Q9BQ39.

KO

K13183.

OMA

GDTEEGC.

OrthoDB

EOG46143T.

PhylomeDB

Q9BQ39.

Gene expression databases

ArrayExpress

Q9BQ39.

Bgee

Q9BQ39.

CleanEx

HS_DDX50.

Genevestigator

Q9BQ39.

Family and domain databases

InterPro

IPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR012562. GUCT.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]

Pfam

PF00270. DEAD. 1 hit.
PF08152. GUCT. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF52540. SSF52540. 2 hits.

PROSITE

PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

DDX50. human.

EvolutionaryTrace

Q9BQ39.

GenomeRNAi

79009.

NextBio

67657.

SOURCE

Search...

Entry information

Entry name

DDX50_HUMAN

Accession

Primary (citable) accession number: Q9BQ39
Secondary accession number(s): Q5VX37, Q8WV76, Q9BWI8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 23, 2004
Last sequence update:	June 1, 2001
Last modified:	May 29, 2013
This is version 108 of the entry and version 1 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.