Q9NR30 (DDX21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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 › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	783 AA.
Sequence status	Complete.
Protein existence	Evidence 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.21
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.

Ontologies

Keywords
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding RNA-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Traceable author statement Ref.1. Source: GOC osteoblast differentiation Inferred from direct assay PubMed 16210410. Source: UniProt response to exogenous dsRNA Inferred from electronic annotation. Source: Ensembl response to virus Inferred from electronic annotation. Source: Ensembl
Cellular_component	membrane Inferred from direct assay PubMed 16210410. Source: UniProt nucleolus Inferred from direct assay. Source: HPA nucleus Inferred from direct assay. Source: HPA
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW ATP-dependent RNA helicase activity Traceable author statement Ref.1. Source: ProtInc double-stranded RNA binding Inferred from electronic annotation. Source: Ensembl poly(A) RNA binding Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 783

783

Nucleolar RNA helicase 2

PRO_0000055027

Regions

Domain

217 – 396

180

Helicase ATP-binding

Domain

429 – 573

145

Helicase C-terminal

Repeat

724 – 728

5

1

Repeat

734 – 738

5

2

Repeat

744 – 748

5

3

Nucleotide binding

230 – 237

8

ATP By similarity

Region

724 – 748

25

3 X 5 AA repeats

Motif

186 – 214

29

Q motif

Motif

339 – 342

4

DEVD box

Amino acid modifications

Modified residue

13

1

Phosphoserine Ref.14 Ref.17 Ref.19 Ref.22

Modified residue

71

1

Phosphoserine Ref.11 Ref.14 Ref.19 Ref.22

Modified residue

89

1

Phosphoserine Ref.11 Ref.13 Ref.14 Ref.19 Ref.22

Modified residue

121

1

Phosphoserine Ref.8 Ref.11 Ref.16 Ref.17 Ref.19 Ref.22

Modified residue

147

1

Phosphoserine By similarity

Modified residue

171

1

Phosphoserine By similarity

Modified residue

296

1

Phosphothreonine Ref.19

Modified residue

567

1

Phosphoserine Ref.19

Modified residue

779

1

N6-acetyllysine Ref.18

Natural variations

Alternative sequence

1 – 68

68

Missing in isoform 2.

VSP_015716

Natural variant

27

1

T → I. Ref.1 Ref.2
Corresponds to variant rs17556220 [ dbSNP | Ensembl ].

VAR_052161

Experimental info

Sequence conflict

273

1

A → C Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

783

Helix Strand Turn

Details...

Beta strand

631 – 642

12

Helix

651 – 660

10

Turn

664 – 667

4

Helix

676 – 678

3

Beta strand

679 – 686

8

Helix

687 – 693

7

Beta strand

704 – 707

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified September 27, 2005. Version 5. Checksum: 4F6673E38686644F	FASTA	783	87,344
	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
	Isoform 2 [UniParc]. Checksum: 8CB8E8BE914EA9DB	FASTA	715	79,657
	10 20 30 40 50 60 MNSPKSKKAK KKEEPSQNDI SPKTKSLRKK KEPIEKKVVS SKTKKVTKNE EPSEEEIDAP 70 80 90 100 110 120 KPKKMKKEKE MNGETREKSP KLKNGFPHPE PDCNPSEAAS EESNSEIEQE IPVEQKEGAF 130 140 150 160 170 180 SNFPISEETI KLLKGRGVTF LFPIQAKTFH HVYSGKDLIA QARTGTGKTF SFAIPLIEKL 190 200 210 220 230 240 HGELQDRKRG RAPQVLVLAP TRELANQVSK DFSDITKKLS VACFYGGTPY GGQFERMRNG 250 260 270 280 290 300 IDILVGTPGR IKDHIQNGKL DLTKLKHVVL DEVDQMLDMG FADQVEEILS VAYKKDSEDN 310 320 330 340 350 360 PQTLLFSATC PHWVFNVAKK YMKSTYEQVD LIGKKTQKTA ITVEHLAIKC HWTQRAAVIG 370 380 390 400 410 420 DVIRVYSGHQ GRTIIFCETK KEAQELSQNS AIKQDAQSLH GDIPQKQREI TLKGFRNGSF 430 440 450 460 470 480 GVLVATNVAA RGLDIPEVDL VIQSSPPKDV ESYIHRSGRT GRAGRTGVCI CFYQHKEEYQ 490 500 510 520 530 540 LVQVEQKAGI KFKRIGVPSA TEIIKASSKD AIRLLDSVPP TAISHFKQSA EKLIEEKGAV 550 560 570 580 590 600 EALAAALAHI SGATSVDQRS LINSNVGFVT MILQCSIEMP NISYAWKELK EQLGEEIDSK 610 620 630 640 650 660 VKGMVFLKGK LGVCFDVPTA SVTEIQEKWH DSRRWQLSVA TEQPELEGPR EGYGGFRGQR 670 680 690 700 710 EGSRGFRGQR DGNRRFRGQR EGSRGPRGQR SGGGNKSNRS QNKGQKRSFS KAFGQ

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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(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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[15]	"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(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[18]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[20]	"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].
[21]	"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.
[22]	"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]	"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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 , 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.

CCDS

CCDS31211.1. [Q9NR30-1]

PIR

PC6010.

RefSeq

NP_001243839.1. NM_001256910.1. [Q9NR30-2]
NP_004719.2. NM_004728.3. [Q9NR30-1]

UniGene

Hs.223141.

3D structure databases

PDBe
RCSB-PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2M3D	NMR	-	A	617-710	[»]

ProteinModelPortal

Q9NR30.

SMR

Q9NR30. Positions 148-710.

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

114625. 104 interactions.

IntAct

Q9NR30. 33 interactions.

MINT

MINT-231639.

STRING

9606.ENSP00000346120.

PTM databases

PhosphoSite

Q9NR30.

Polymorphism databases

DMDM

76803555.

2D gel databases

SWISS-2DPAGE

Q9NR30.

Proteomic databases

MaxQB

Q9NR30.

PaxDb

Q9NR30.

PeptideAtlas

Q9NR30.

PRIDE

Q9NR30.

Protocols and materials databases

DNASU

9188.

StructuralBiologyKnowledgebase

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Genome annotation databases

Ensembl

ENST00000354185; ENSP00000346120; ENSG00000165732. [Q9NR30-1]

GeneID

9188.

KEGG

hsa:9188.

UCSC

uc001jov.2. human. [Q9NR30-1]

Organism-specific databases

CTD

9188.

GeneCards

GC10P070715.

H-InvDB

HIX0008880.

HGNC

HGNC:2744. DDX21.

HPA

HPA036592.
HPA036593.

MIM

606357. gene.

neXtProt

NX_Q9NR30.

PharmGKB

PA27210.

GenAtlas

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Phylogenomic databases

eggNOG

COG0513.

HOGENOM

HOG000268805.

HOVERGEN

HBG051331.

InParanoid

Q9NR30.

KO

K16911.

OMA

SQNDISP.

OrthoDB

EOG77HDD6.

PhylomeDB

Q9NR30.

TreeFam

TF328622.

Gene expression databases

ArrayExpress

Q9NR30.

Bgee

Q9NR30.

CleanEx

HS_DDX21.

Genevestigator

Q9NR30.

Family and domain databases

Gene3D

3.40.50.300. 2 hits.

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. 3 hits.

PROSITE

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

ProtoNet

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Other

ChiTaRS

DDX21. human.

GeneWiki

DDX21.

GenomeRNAi

9188.

NextBio

34453.

PRO

Q9NR30.

SOURCE

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Entry information

Entry name

DDX21_HUMAN

Accession

Primary (citable) accession number: Q9NR30
Secondary accession number(s): B2RDL0 , Q13436, Q5VX41, Q68D35

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	September 27, 2005
Last modified:	July 9, 2014
This is version 154 of the entry and version 5 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.