Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9NR30 (DDX21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Nucleolar RNA helicase 2
EC=3.6.4.13
Alternative name(s):
DEAD box protein 21
Gu-alpha
Nucleolar RNA helicase Gu
Nucleolar RNA helicase II
RH II/Gu
Gene names
Name:DDX21
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length783 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase). Functions as cofactor for JUN-activated transcription. Involved in rRNA processing. Ref.9 Ref.10

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with C1QBP. Ref.12 Ref.20

Subcellular location

Nucleus › nucleolus Ref.1.

Domain

The two enzymatic activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus.

The 3 X 5 AA repeats seem to be critical for the RNA folding activity By similarity.

Miscellaneous

Autoantibodies against DDX21 are found in patients with watermelon stomach disease, which is characterized by prominent stripes of ectatic vascular tissue in the stomach similar to stripes on a watermelon.

Sequence similarities

Belongs to the DEAD box helicase family. DDX21/DDX50 subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Sequence caution

The sequence AAB02546.1 differs from that shown. Reason: Erroneous initiation.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NR30-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NR30-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-68: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 783783Nucleolar RNA helicase 2
PRO_0000055027

Regions

Domain217 – 396180Helicase ATP-binding
Domain429 – 573145Helicase C-terminal
Repeat724 – 72851
Repeat734 – 73852
Repeat744 – 74853
Nucleotide binding230 – 2378ATP By similarity
Region724 – 748253 X 5 AA repeats
Motif186 – 21429Q motif
Motif339 – 3424DEVD box

Amino acid modifications

Modified residue131Phosphoserine Ref.14 Ref.16 Ref.18 Ref.21
Modified residue711Phosphoserine Ref.11 Ref.14 Ref.18 Ref.21
Modified residue891Phosphoserine Ref.11 Ref.13 Ref.14 Ref.18 Ref.21
Modified residue1211Phosphoserine Ref.8 Ref.11 Ref.15 Ref.16 Ref.18 Ref.21
Modified residue1471Phosphoserine By similarity
Modified residue1641Phosphoserine By similarity
Modified residue1731Phosphoserine By similarity
Modified residue1891Phosphoserine By similarity
Modified residue2961Phosphothreonine Ref.18
Modified residue5671Phosphoserine Ref.18
Modified residue7791N6-acetyllysine Ref.17

Natural variations

Alternative sequence1 – 6868Missing in isoform 2.
VSP_015716
Natural variant271T → I. Ref.1 Ref.2
Corresponds to variant rs17556220 [ dbSNP | Ensembl ].
VAR_052161

Experimental info

Sequence conflict2731A → C Ref.2

Secondary structure

1 ............. 783
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified September 27, 2005. Version 5.
Checksum: 4F6673E38686644F

FASTA78387,344
        10         20         30         40         50         60 
MPGKLRSDAG LESDTAMKKG ETLRKQTEEK EKKEKPKSDK TEEIAEEEET VFPKAKQVKK 

        70         80         90        100        110        120 
KAEPSEVDMN SPKSKKAKKK EEPSQNDISP KTKSLRKKKE PIEKKVVSSK TKKVTKNEEP 

       130        140        150        160        170        180 
SEEEIDAPKP KKMKKEKEMN GETREKSPKL KNGFPHPEPD CNPSEAASEE SNSEIEQEIP 

       190        200        210        220        230        240 
VEQKEGAFSN FPISEETIKL LKGRGVTFLF PIQAKTFHHV YSGKDLIAQA RTGTGKTFSF 

       250        260        270        280        290        300 
AIPLIEKLHG ELQDRKRGRA PQVLVLAPTR ELANQVSKDF SDITKKLSVA CFYGGTPYGG 

       310        320        330        340        350        360 
QFERMRNGID ILVGTPGRIK DHIQNGKLDL TKLKHVVLDE VDQMLDMGFA DQVEEILSVA 

       370        380        390        400        410        420 
YKKDSEDNPQ TLLFSATCPH WVFNVAKKYM KSTYEQVDLI GKKTQKTAIT VEHLAIKCHW 

       430        440        450        460        470        480 
TQRAAVIGDV IRVYSGHQGR TIIFCETKKE AQELSQNSAI KQDAQSLHGD IPQKQREITL 

       490        500        510        520        530        540 
KGFRNGSFGV LVATNVAARG LDIPEVDLVI QSSPPKDVES YIHRSGRTGR AGRTGVCICF 

       550        560        570        580        590        600 
YQHKEEYQLV QVEQKAGIKF KRIGVPSATE IIKASSKDAI RLLDSVPPTA ISHFKQSAEK 

       610        620        630        640        650        660 
LIEEKGAVEA LAAALAHISG ATSVDQRSLI NSNVGFVTMI LQCSIEMPNI SYAWKELKEQ 

       670        680        690        700        710        720 
LGEEIDSKVK GMVFLKGKLG VCFDVPTASV TEIQEKWHDS RRWQLSVATE QPELEGPREG 

       730        740        750        760        770        780 
YGGFRGQREG SRGFRGQRDG NRRFRGQREG SRGPRGQRSG GGNKSNRSQN KGQKRSFSKA 


FGQ

« Hide

Isoform 2 [UniParc].

Checksum: 8CB8E8BE914EA9DB
Show »

FASTA71579,657

References

« Hide 'large scale' references
[1]"A nucleolar RNA helicase recognized by autoimmune antibodies from a patient with watermelon stomach disease."
Valdez B.C., Henning D., Busch R.K., Woods K., Flores-Rozas H., Hurwitz J., Perlaky L., Busch H.
Nucleic Acids Res. 24:1220-1224(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, VARIANT ILE-27.
[2]"Human RNA helicase II/Gu gene: genomic organization and promoter analysis."
Zhu K., Henning D., Valdez B.C., Busch H.
Biochem. Biophys. Res. Commun. 281:1006-1011(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-27.
Tissue: Cervix adenocarcinoma.
[3]"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] (ISOFORM 2).
Tissue: Placenta.
[4]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Uterine endothelium.
[5]"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. expand/collapse author list , 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].
[6]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].
[7]"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] (ISOFORM 1).
Tissue: Colon and Muscle.
[8]Bienvenut W.V., Waridel P., Quadroni M.
Submitted (MAR-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 7-18; 117-131; 185-199; 205-215; 237-247; 258-270; 287-304; 307-318; 364-387; 392-402; 407-417; 424-432; 450-474; 485-499; 545-555; 606-627; 659-668; 679-696 AND 703-718, PHOSPHORYLATION AT SER-121, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[9]"The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription."
Westermarck J., Weiss C., Saffrich R., Kast J., Musti A.M., Wessely M., Ansorge W., Seraphin B., Wilm M., Valdez B.C., Bohmann D.
EMBO J. 21:451-460(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 185-199; 260-270 AND 563-573, FUNCTION.
[10]"Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA production."
Henning D., So R.B., Jin R., Lau L.F., Valdez B.C.
J. Biol. Chem. 278:52307-52314(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[12]"The WSTF-SNF2h chromatin remodeling complex interacts with several nuclear proteins in transcription."
Cavellan E., Asp P., Percipalle P., Oestlund Farrants A.-K.
J. Biol. Chem. 281:16264-16271(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
[13]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[14]"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-13; SER-71 AND SER-89, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[15]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, MASS SPECTROMETRY.
[16]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-121, MASS SPECTROMETRY.
Tissue: Leukemic T-cell.
[17]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779, MASS SPECTROMETRY.
[18]"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-13; SER-71; SER-89; SER-121; THR-296 AND SER-567, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[19]"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].
[20]"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.
[21]"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-13; SER-71; SER-89 AND SER-121, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U41387 mRNA. Translation: AAB02546.1. Different initiation.
AF261903 Genomic DNA. No translation available.
AF261917 expand/collapse EMBL AC list , AF261904, AF261905, AF261906, AF261907, AF261908, AF261909, AF261910, AF261911, AF261912, AF261913, AF261914, AF261915, AF261916 Genomic DNA. Translation: AAF78930.2.
AK315585 mRNA. Translation: BAG37957.1.
CR749598 mRNA. Translation: CAH18395.1.
AL359844 Genomic DNA. Translation: CAH72377.1.
CH471083 Genomic DNA. Translation: EAW54307.1.
BC008071 mRNA. Translation: AAH08071.2.
IPIIPI00015953.
IPI00477179.
PIRPC6010.
RefSeqNP_001243839.1. NM_001256910.1.
NP_004719.2. NM_004728.3.
UniGeneHs.223141.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2M3DNMR-A617-710[»]
ProteinModelPortalQ9NR30.
ModBaseSearch...

Protein-protein interaction databases

IntActQ9NR30. 23 interactions.
MINTMINT-231639.
STRING9606.ENSP00000346120.

PTM databases

PhosphoSiteQ9NR30.

Polymorphism databases

DMDM76803555.

2D gel databases

SWISS-2DPAGEQ9NR30.

Proteomic databases

PaxDbQ9NR30.
PeptideAtlasQ9NR30.
PRIDEQ9NR30.

Protocols and materials databases

DNASU9188.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000354185; ENSP00000346120; ENSG00000165732.
GeneID9188.
KEGGhsa:9188.
UCSCuc001jov.1. human.

Organism-specific databases

CTD9188.
GeneCardsGC10P070715.
H-InvDBHIX0008880.
HGNCHGNC:2744. DDX21.
HPAHPA036592.
MIM606357. gene.
neXtProtNX_Q9NR30.
PharmGKBPA27210.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0513.
HOGENOMHOG000268805.
HOVERGENHBG051331.
InParanoidQ9NR30.
OMAEILCVAY.
OrthoDBEOG46143T.
PhylomeDBQ9NR30.

Gene expression databases

ArrayExpressQ9NR30.
BgeeQ9NR30.
CleanExHS_DDX21.
GenevestigatorQ9NR30.
GermOnlineENSG00000165732. Homo sapiens.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR012562. GUCT.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF08152. GUCT. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
PROSITEPS00039. DEAD_ATP_HELICASE. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDDX21. human.
GenomeRNAi9188.
NextBio34453.
SOURCESearch...

Entry information

Entry nameDDX21_HUMAN
AccessionPrimary (citable) accession number: Q9NR30
Secondary accession number(s): B2RDL0 expand/collapse secondary AC list , Q13436, Q5VX41, Q68D35
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 27, 2005
Last modified: May 1, 2013
This is version 141 of the entry and version 5 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

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents