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Protein

Nucleolar RNA helicase 2

Gene

DDX21

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

Functioni

RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Involved in rRNA processing (PubMed:14559904, PubMed:18180292).7 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi230 – 2378ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. ATP-dependent RNA helicase activity Source: ProtInc
  3. double-stranded RNA binding Source: Ensembl
  4. poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: GOC
  2. osteoblast differentiation Source: UniProtKB
  3. response to exogenous dsRNA Source: Ensembl
  4. response to virus Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

rRNA processing, Transcription

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Nucleolar RNA helicase 2Curated (EC:3.6.4.131 Publication)
Alternative name(s):
DEAD box protein 21
Gu-alpha
Nucleolar RNA helicase Gu
Nucleolar RNA helicase II
RH II/Gu
Gene namesi
Name:DDX21
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:2744. DDX21.

Subcellular locationi

Nucleusnucleolus 6 Publications. Nucleusnucleoplasm 4 Publications
Note: Present both in nucleolus and nucleoplasm. Interaction with JUN promotes translocation from the nucleolus to the nucleoplasm (PubMed:11823437, PubMed:18180292). Interaction with WDR46 is required for localization to the nucleolus (PubMed:23848194).3 Publications

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi339 – 3402DE → HG in mutant DEV; loss of helicase activity. Defects in release of P-TEFb from inhibitory 7SK snRNP. 2 Publications
Mutagenesisi375 – 3762SA → LE in mutant SAT; ATPase defective. Defects in release of P-TEFb from inhibitory 7SK snRNP. 2 Publications

Organism-specific databases

PharmGKBiPA27210.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 783783Nucleolar RNA helicase 2PRO_0000055027Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei13 – 131Phosphoserine4 Publications
Modified residuei71 – 711Phosphoserine4 Publications
Modified residuei89 – 891Phosphoserine5 Publications
Modified residuei121 – 1211Phosphoserine6 Publications
Modified residuei147 – 1471PhosphoserineBy similarity
Modified residuei171 – 1711PhosphoserineBy similarity
Modified residuei296 – 2961Phosphothreonine1 Publication
Modified residuei567 – 5671Phosphoserine1 Publication
Modified residuei779 – 7791N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9NR30.
PaxDbiQ9NR30.
PeptideAtlasiQ9NR30.
PRIDEiQ9NR30.

2D gel databases

SWISS-2DPAGEQ9NR30.

PTM databases

PhosphoSiteiQ9NR30.

Expressioni

Gene expression databases

BgeeiQ9NR30.
CleanExiHS_DDX21.
ExpressionAtlasiQ9NR30. baseline and differential.
GenevestigatoriQ9NR30.

Organism-specific databases

HPAiHPA036592.
HPA036593.

Interactioni

Subunit structurei

Component of the B-WICH complex, at least composed of SMARCA5/SNF2H, BAZ1B/WSTF, SF3B1, DEK, MYO1C, ERCC6, MYBBP1A and DDX21. Interacts with C1QBP. Interacts with JUN (PubMed:11823437, PubMed:18180292). Interacts with WDR46 (PubMed:23848194).5 Publications

Protein-protein interaction databases

BioGridi114625. 110 interactions.
IntActiQ9NR30. 33 interactions.
MINTiMINT-231639.
STRINGi9606.ENSP00000346120.

Structurei

Secondary structure

1
783
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi631 – 64212Combined sources
Helixi651 – 66010Combined sources
Turni664 – 6674Combined sources
Helixi676 – 6783Combined sources
Beta strandi679 – 6868Combined sources
Helixi687 – 6937Combined sources
Beta strandi704 – 7074Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M3DNMR-A617-710[»]
ProteinModelPortaliQ9NR30.
SMRiQ9NR30. Positions 148-710.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini217 – 396180Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini429 – 573145Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST
Repeati724 – 72851
Repeati734 – 73852
Repeati744 – 74853

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni724 – 748253 X 5 AA repeatsAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi186 – 21429Q motifPROSITE-ProRule annotationAdd
BLAST
Motifi339 – 3424DEAD boxPROSITE-ProRule annotation

Domaini

The helicase and foldase activities reside in two separate domains, the helicase in the N-terminus and the foldase in the C-terminus.1 Publication
The 3 X 5 AA repeats seem to be critical for the RNA folding activity.By similarity

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00780000121987.
HOGENOMiHOG000268805.
HOVERGENiHBG051331.
InParanoidiQ9NR30.
KOiK16911.
OMAiSQNDISP.
OrthoDBiEOG77HDD6.
PhylomeDBiQ9NR30.
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. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9NR30-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MPGKLRSDAG LESDTAMKKG ETLRKQTEEK EKKEKPKSDK TEEIAEEEET
60 70 80 90 100
VFPKAKQVKK KAEPSEVDMN SPKSKKAKKK EEPSQNDISP KTKSLRKKKE
110 120 130 140 150
PIEKKVVSSK TKKVTKNEEP SEEEIDAPKP KKMKKEKEMN GETREKSPKL
160 170 180 190 200
KNGFPHPEPD CNPSEAASEE SNSEIEQEIP VEQKEGAFSN FPISEETIKL
210 220 230 240 250
LKGRGVTFLF PIQAKTFHHV YSGKDLIAQA RTGTGKTFSF AIPLIEKLHG
260 270 280 290 300
ELQDRKRGRA PQVLVLAPTR ELANQVSKDF SDITKKLSVA CFYGGTPYGG
310 320 330 340 350
QFERMRNGID ILVGTPGRIK DHIQNGKLDL TKLKHVVLDE VDQMLDMGFA
360 370 380 390 400
DQVEEILSVA YKKDSEDNPQ TLLFSATCPH WVFNVAKKYM KSTYEQVDLI
410 420 430 440 450
GKKTQKTAIT VEHLAIKCHW TQRAAVIGDV IRVYSGHQGR TIIFCETKKE
460 470 480 490 500
AQELSQNSAI KQDAQSLHGD IPQKQREITL KGFRNGSFGV LVATNVAARG
510 520 530 540 550
LDIPEVDLVI QSSPPKDVES YIHRSGRTGR AGRTGVCICF YQHKEEYQLV
560 570 580 590 600
QVEQKAGIKF KRIGVPSATE IIKASSKDAI RLLDSVPPTA ISHFKQSAEK
610 620 630 640 650
LIEEKGAVEA LAAALAHISG ATSVDQRSLI NSNVGFVTMI LQCSIEMPNI
660 670 680 690 700
SYAWKELKEQ LGEEIDSKVK GMVFLKGKLG VCFDVPTASV TEIQEKWHDS
710 720 730 740 750
RRWQLSVATE QPELEGPREG YGGFRGQREG SRGFRGQRDG NRRFRGQREG
760 770 780
SRGPRGQRSG GGNKSNRSQN KGQKRSFSKA FGQ
Length:783
Mass (Da):87,344
Last modified:September 27, 2005 - v5
Checksum:i4F6673E38686644F
GO
Isoform 2 (identifier: Q9NR30-2) [UniParc]FASTAAdd to basket

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

Note: Contains a N-acetylmethionine at position 1.1 Publication

Show »
Length:715
Mass (Da):79,657
Checksum:i8CB8E8BE914EA9DB
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti273 – 2731A → C in AAF78930 (PubMed:11237763).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti27 – 271T → I.2 Publications
Corresponds to variant rs17556220 [ dbSNP | Ensembl ].
VAR_052161

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6868Missing in isoform 2. 2 PublicationsVSP_015716Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41387 mRNA. Translation: AAB02546.1. Different initiation.
AF261903 Genomic DNA. No translation available.
AF261917
, 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.
CCDSiCCDS31211.1. [Q9NR30-1]
CCDS73144.1. [Q9NR30-2]
PIRiPC6010.
RefSeqiNP_001243839.1. NM_001256910.1. [Q9NR30-2]
NP_004719.2. NM_004728.3. [Q9NR30-1]
UniGeneiHs.223141.

Genome annotation databases

EnsembliENST00000354185; ENSP00000346120; ENSG00000165732. [Q9NR30-1]
ENST00000620315; ENSP00000480334; ENSG00000165732. [Q9NR30-2]
GeneIDi9188.
KEGGihsa:9188.
UCSCiuc001jov.2. human. [Q9NR30-1]

Polymorphism databases

DMDMi76803555.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U41387 mRNA. Translation: AAB02546.1. Different initiation.
AF261903 Genomic DNA. No translation available.
AF261917
, 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.
CCDSiCCDS31211.1. [Q9NR30-1]
CCDS73144.1. [Q9NR30-2]
PIRiPC6010.
RefSeqiNP_001243839.1. NM_001256910.1. [Q9NR30-2]
NP_004719.2. NM_004728.3. [Q9NR30-1]
UniGeneiHs.223141.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2M3DNMR-A617-710[»]
ProteinModelPortaliQ9NR30.
SMRiQ9NR30. Positions 148-710.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114625. 110 interactions.
IntActiQ9NR30. 33 interactions.
MINTiMINT-231639.
STRINGi9606.ENSP00000346120.

PTM databases

PhosphoSiteiQ9NR30.

Polymorphism databases

DMDMi76803555.

2D gel databases

SWISS-2DPAGEQ9NR30.

Proteomic databases

MaxQBiQ9NR30.
PaxDbiQ9NR30.
PeptideAtlasiQ9NR30.
PRIDEiQ9NR30.

Protocols and materials databases

DNASUi9188.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354185; ENSP00000346120; ENSG00000165732. [Q9NR30-1]
ENST00000620315; ENSP00000480334; ENSG00000165732. [Q9NR30-2]
GeneIDi9188.
KEGGihsa:9188.
UCSCiuc001jov.2. human. [Q9NR30-1]

Organism-specific databases

CTDi9188.
GeneCardsiGC10P070715.
H-InvDBHIX0008880.
HGNCiHGNC:2744. DDX21.
HPAiHPA036592.
HPA036593.
MIMi606357. gene.
neXtProtiNX_Q9NR30.
PharmGKBiPA27210.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00780000121987.
HOGENOMiHOG000268805.
HOVERGENiHBG051331.
InParanoidiQ9NR30.
KOiK16911.
OMAiSQNDISP.
OrthoDBiEOG77HDD6.
PhylomeDBiQ9NR30.
TreeFamiTF328622.

Miscellaneous databases

ChiTaRSiDDX21. human.
GeneWikiiDDX21.
GenomeRNAii9188.
NextBioi34453.
PROiQ9NR30.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NR30.
CleanExiHS_DDX21.
ExpressionAtlasiQ9NR30. baseline and differential.
GenevestigatoriQ9NR30.

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. 3 hits.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1995) [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(2000) [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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  4. 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.
    , 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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. 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(2003) [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 (FEB-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, IDENTIFICATION BY 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(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 185-199; 260-270 AND 563-573, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH JUN.
  10. "RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two activities in separate domains of the same protein."
    Valdez B.C., Henning D., Perumal K., Busch H.
    Eur. J. Biochem. 250:800-807(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
  11. "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(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71; SER-89 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE B-WICH COMPLEX.
  14. "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(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: FUNCTION, SUBCELLULAR LOCATION.
  16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71 AND SER-89, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-779, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "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(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71; SER-89; SER-121; THR-296 AND SER-567, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH C1QBP.
  24. "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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13; SER-71; SER-89 AND SER-121, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "Nucleolar scaffold protein, WDR46, determines the granular compartmental localization of nucleolin and DDX21."
    Hirai Y., Louvet E., Oda T., Kumeta M., Watanabe Y., Horigome T., Takeyasu K.
    Genes Cells 18:780-797(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH WDR46.
  27. "Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers."
    Zhang Y., Baysac K.C., Yee L.F., Saporita A.J., Weber J.D.
    Breast Cancer Res. 16:449-449(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "RNA helicase DDX21 coordinates transcription and ribosomal RNA processing."
    Calo E., Flynn R.A., Martin L., Spitale R.C., Chang H.Y., Wysocka J.
    Nature 518:249-253(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF 339-ASP-GLU-340 AND 375-SER-ALA-376.
  30. Cited for: FUNCTION, RNA-BINDING.
  31. "NMR structure of the GUCT domain from human DEAD box polypeptide 21 (DDX21)."
    Dutta S.K., Serrano P., Geralt M., Wuthrich K.
    Submitted (DEC-2012) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 617-710.

Entry informationi

Entry nameiDDX21_HUMAN
AccessioniPrimary (citable) accession number: Q9NR30
Secondary accession number(s): B2RDL0
, Q13436, Q5VX41, Q68D35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: September 27, 2005
Last modified: April 1, 2015
This is version 162 of the entry and version 5 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

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.1 Publication

Keywords - Technical termi

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

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.