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Protein

Putative ATP-dependent RNA helicase DHX33

Gene

Dhx33

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi88 – 958ATPPROSITE-ProRule annotation

GO - Molecular functioni

  • activating transcription factor binding Source: UniProtKB
  • ATP binding Source: UniProtKB-KW
  • ATP-dependent RNA helicase activity Source: GO_Central
  • poly(A) RNA binding Source: MGI
  • rDNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative ATP-dependent RNA helicase DHX33 (EC:3.6.4.13)
Alternative name(s):
DEAH box protein 33
Gene namesi
Name:Dhx33
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2445102. Dhx33.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • nucleolus Source: UniProtKB
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi94 – 941K → N or R: Loss of stimulation of rRNA synthesis. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 698698Putative ATP-dependent RNA helicase DHX33PRO_0000055165Add
BLAST

Proteomic databases

MaxQBiQ80VY9.
PRIDEiQ80VY9.

PTM databases

PhosphoSiteiQ80VY9.

Expressioni

Gene expression databases

BgeeiQ80VY9.
CleanExiMM_DHX33.
ExpressionAtlasiQ80VY9. baseline and differential.
GenevisibleiQ80VY9. MM.

Interactioni

Subunit structurei

Interacts with UBTF.1 Publication

Protein-protein interaction databases

BioGridi229816. 1 interaction.
STRINGi10090.ENSMUSP00000104167.

Structurei

3D structure databases

ProteinModelPortaliQ80VY9.
SMRiQ80VY9. Positions 62-689.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini75 – 243169Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini271 – 441171Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi185 – 1884DEAH box
Motifi536 – 55015Critical for rDNA-bindingAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1643.
GeneTreeiENSGT00770000120489.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiQ80VY9.
KOiK17820.
OMAiPMGRKMA.
OrthoDBiEOG718KC0.
PhylomeDBiQ80VY9.
TreeFamiTF354245.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q80VY9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEEASLPPA KRFRPGSCPP GRRVVMLLTA GGGGGAGGGR RQTPPLAQPS
60 70 80 90 100
ASPYREALEL QRRSLPIFRA RGQLLAQLRN LDNAVLIGET GSGKTTQIPQ
110 120 130 140 150
YLYEGGISRQ GIIAVTQPRR VAAISLATRV SDEKRTELGK LVGYTVRFED
160 170 180 190 200
VTSEDTRIKF LTDGMLLREA ISDSLLRKYS CVILDEAHER TIHTDVLFGV
210 220 230 240 250
VKTAQKRRKE LGKLPLKVIV MSATMDVDLF SQYFNRAPVL YLEGRQHPIQ
260 270 280 290 300
IFYTKQPQQD YLHAALVSVF QIHQEAPASQ DILVFLTGQE EIEAMSKTCR
310 320 330 340 350
DIARHLPDGC PSMLVLPLYA SLPYSQQLRV FQGAPKGYRK VIISTNIAET
360 370 380 390 400
SITITGIKYV VDTGMVKAKK YNPDSGLEVL AVQRVSKTQA WQRTGRAGRE
410 420 430 440 450
DSGICYRLYT EDEFEKFEKM TVPEIQRCNL ASVILQLLAM KVPNVLTFDF
460 470 480 490 500
MSKPSPDHIE AAIAQLDLLG ALEHKDDQLT LTPIGRKMAA FPLEPRFAKT
510 520 530 540 550
ILLSSKFHCT EEILTIVSLL SVDSVLYNPP ARRDEVQSVR KKFISSEGDH
560 570 580 590 600
ITLLNIYRTF KNIGGNKDWC KENFVNSKNM LLVAEVRAQL REICLKMSMP
610 620 630 640 650
IMSSRGDMES VRRCMAHSLF MNTAELQTDG TYATTDTHQP VAIHPSSVLF
660 670 680 690
HCKPACVVYT SLLYTNKCYM RDLCVVDAEW LYEAAPDYFR RKLRTARN
Length:698
Mass (Da):78,347
Last modified:June 1, 2003 - v1
Checksum:i7DFF1F220C69544E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti470 – 4701G → V in BAC28969 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035177 mRNA. Translation: BAC28969.1.
BC052172 mRNA. Translation: AAH52172.1.
CCDSiCCDS24971.1.
RefSeqiNP_848144.3. NM_178367.4.
UniGeneiMm.35399.

Genome annotation databases

EnsembliENSMUST00000108527; ENSMUSP00000104167; ENSMUSG00000040620.
GeneIDi216877.
KEGGimmu:216877.
UCSCiuc007jxg.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK035177 mRNA. Translation: BAC28969.1.
BC052172 mRNA. Translation: AAH52172.1.
CCDSiCCDS24971.1.
RefSeqiNP_848144.3. NM_178367.4.
UniGeneiMm.35399.

3D structure databases

ProteinModelPortaliQ80VY9.
SMRiQ80VY9. Positions 62-689.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi229816. 1 interaction.
STRINGi10090.ENSMUSP00000104167.

PTM databases

PhosphoSiteiQ80VY9.

Proteomic databases

MaxQBiQ80VY9.
PRIDEiQ80VY9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000108527; ENSMUSP00000104167; ENSMUSG00000040620.
GeneIDi216877.
KEGGimmu:216877.
UCSCiuc007jxg.1. mouse.

Organism-specific databases

CTDi56919.
MGIiMGI:2445102. Dhx33.

Phylogenomic databases

eggNOGiCOG1643.
GeneTreeiENSGT00770000120489.
HOGENOMiHOG000175261.
HOVERGENiHBG039428.
InParanoidiQ80VY9.
KOiK17820.
OMAiPMGRKMA.
OrthoDBiEOG718KC0.
PhylomeDBiQ80VY9.
TreeFamiTF354245.

Miscellaneous databases

ChiTaRSiDhx33. mouse.
NextBioi375442.
PROiQ80VY9.
SOURCEiSearch...

Gene expression databases

BgeeiQ80VY9.
CleanExiMM_DHX33.
ExpressionAtlasiQ80VY9. baseline and differential.
GenevisibleiQ80VY9. MM.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR002464. DNA/RNA_helicase_DEAH_CS.
IPR011709. DUF1605.
IPR007502. Helicase-assoc_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF04408. HA2. 1 hit.
PF00271. Helicase_C. 1 hit.
PF07717. OB_NTP_bind. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00847. HA2. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS00690. DEAH_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. "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.

Entry informationi

Entry nameiDHX33_MOUSE
AccessioniPrimary (citable) accession number: Q80VY9
Secondary accession number(s): Q8BS50
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 22, 2005
Last sequence update: June 1, 2003
Last modified: June 24, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.