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Q80VY9 (DHX33_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 87. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative ATP-dependent RNA helicase DHX33
EC=3.6.4.13
Alternative name(s):
DEAH box protein 33
Gene names
Name:Dhx33
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length698 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Stimulates RNA polymerase I transcription of the 47S precursor rRNA. Associates with ribosomal DNA (rDNA) loci where it is involved in POLR1A recruitment. Important element of nucleolar organization By similarity. Ref.4

Catalytic activity

ATP + H2O = ADP + phosphate.

Subunit structure

Interacts with UBTF. Ref.4

Subcellular location

Nucleus › nucleolus. Note: During mitosis, localizes with the nucleolar organizing regions By similarity. Ref.4

Sequence similarities

Belongs to the DEAD box helicase family. DEAH subfamily.

Contains 1 helicase ATP-binding domain.

Contains 1 helicase C-terminal domain.

Ontologies

Keywords
   Cellular componentNucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionHelicase
Hydrolase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processpositive regulation of transcription from RNA polymerase I promoter

Inferred from direct assay Ref.4. Source: UniProtKB

   Cellular_componentnucleolus

Inferred from direct assay Ref.4. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.4. Source: UniProtKB

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATP-dependent helicase activity

Inferred from electronic annotation. Source: InterPro

rDNA binding

Inferred from direct assay Ref.4. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 698698Putative ATP-dependent RNA helicase DHX33
PRO_0000055165

Regions

Domain75 – 243169Helicase ATP-binding
Domain271 – 441171Helicase C-terminal
Nucleotide binding88 – 958ATP By similarity
Motif185 – 1884DEAH box
Motif536 – 55015Critical for rDNA-binding

Amino acid modifications

Modified residue1251Phosphoserine Ref.3

Experimental info

Mutagenesis941K → N or R: Loss of stimulation of rRNA synthesis. Ref.4
Sequence conflict4701G → V in BAC28969. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q80VY9 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 7DFF1F220C69544E

FASTA69878,347
        10         20         30         40         50         60 
MPEEASLPPA KRFRPGSCPP GRRVVMLLTA GGGGGAGGGR RQTPPLAQPS ASPYREALEL 

        70         80         90        100        110        120 
QRRSLPIFRA RGQLLAQLRN LDNAVLIGET GSGKTTQIPQ YLYEGGISRQ GIIAVTQPRR 

       130        140        150        160        170        180 
VAAISLATRV SDEKRTELGK LVGYTVRFED VTSEDTRIKF LTDGMLLREA ISDSLLRKYS 

       190        200        210        220        230        240 
CVILDEAHER TIHTDVLFGV VKTAQKRRKE LGKLPLKVIV MSATMDVDLF SQYFNRAPVL 

       250        260        270        280        290        300 
YLEGRQHPIQ IFYTKQPQQD YLHAALVSVF QIHQEAPASQ DILVFLTGQE EIEAMSKTCR 

       310        320        330        340        350        360 
DIARHLPDGC PSMLVLPLYA SLPYSQQLRV FQGAPKGYRK VIISTNIAET SITITGIKYV 

       370        380        390        400        410        420 
VDTGMVKAKK YNPDSGLEVL AVQRVSKTQA WQRTGRAGRE DSGICYRLYT EDEFEKFEKM 

       430        440        450        460        470        480 
TVPEIQRCNL ASVILQLLAM KVPNVLTFDF MSKPSPDHIE AAIAQLDLLG ALEHKDDQLT 

       490        500        510        520        530        540 
LTPIGRKMAA FPLEPRFAKT ILLSSKFHCT EEILTIVSLL SVDSVLYNPP ARRDEVQSVR 

       550        560        570        580        590        600 
KKFISSEGDH ITLLNIYRTF KNIGGNKDWC KENFVNSKNM LLVAEVRAQL REICLKMSMP 

       610        620        630        640        650        660 
IMSSRGDMES VRRCMAHSLF MNTAELQTDG TYATTDTHQP VAIHPSSVLF HCKPACVVYT 

       670        680        690 
SLLYTNKCYM RDLCVVDAEW LYEAAPDYFR RKLRTARN

« Hide

References

« Hide 'large scale' references
[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Embryo.
[2]"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: Embryonic limb.
[3]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY.
Tissue: Brain cortex.
[4]"Identification of DHX33 as a mediator of rRNA synthesis and cell growth."
Zhang Y., Forys J.T., Miceli A.P., Gwinn A.S., Weber J.D.
Mol. Cell. Biol. 31:4676-4691(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH UBTF, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-94.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK035177 mRNA. Translation: BAC28969.1.
BC052172 mRNA. Translation: AAH52172.1.
IPIIPI00410764.
RefSeqNP_848144.3. NM_178367.4.
UniGeneMm.35399.

3D structure databases

ProteinModelPortalQ80VY9.
SMRQ80VY9. Positions 62-689.
ModBaseSearch...

PTM databases

PhosphoSiteQ80VY9.

Proteomic databases

PRIDEQ80VY9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000108527; ENSMUSP00000104167; ENSMUSG00000040620.
GeneID216877.
KEGGmmu:216877.

Organism-specific databases

CTD56919.
MGIMGI:2445102. Dhx33.

Phylogenomic databases

eggNOGCOG1643.
GeneTreeENSGT00700000104241.
HOGENOMHOG000175261.
HOVERGENHBG039428.
InParanoidQ80VY9.
OMAAPDYFRR.

Gene expression databases

ArrayExpressQ80VY9.
BgeeQ80VY9.
CleanExMM_DHX33.
GenevestigatorQ80VY9.
GermOnlineENSMUSG00000040620. Mus musculus.

Family and domain databases

InterProIPR011545. DNA/RNA_helicase_DEAD/DEAH_N.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
[Graphical view]
PfamPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
PROSITEPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDHX33. mouse.
NextBio375442.
SOURCESearch...

Entry information

Entry nameDHX33_MOUSE
AccessionPrimary (citable) accession number: Q80VY9
Secondary accession number(s): Q8BS50
Entry history
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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