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Q8K301

- DDX52_MOUSE

UniProt

Q8K301 - DDX52_MOUSE

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Protein

Probable ATP-dependent RNA helicase DDX52

Gene

Ddx52

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli

Functioni

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi210 – 2178ATPPROSITE-ProRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. helicase activity Source: UniProtKB-KW
  3. RNA binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Probable ATP-dependent RNA helicase DDX52 (EC:3.6.4.13)
Alternative name(s):
ATP-dependent RNA helicase ROK1-like
DEAD box protein 52
Gene namesi
Name:Ddx52
Synonyms:Rok1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:1925644. Ddx52.

Subcellular locationi

Nucleusnucleolus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Probable ATP-dependent RNA helicase DDX52PRO_0000055061Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151N6-acetyllysineBy similarity
Modified residuei39 – 391PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ8K301.
PaxDbiQ8K301.
PRIDEiQ8K301.

PTM databases

PhosphoSiteiQ8K301.

Expressioni

Gene expression databases

BgeeiQ8K301.
CleanExiMM_DDX52.
ExpressionAtlasiQ8K301. baseline and differential.
GenevestigatoriQ8K301.

Interactioni

Protein-protein interaction databases

BioGridi219368. 1 interaction.
STRINGi10090.ENSMUSP00000048802.

Structurei

3D structure databases

ProteinModelPortaliQ8K301.
SMRiQ8K301. Positions 140-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini197 – 375179Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini386 – 547162Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi166 – 19429Q motifAdd
BLAST
Motifi319 – 3224DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi86 – 927Poly-Lys

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00550000074863.
HOGENOMiHOG000242486.
HOVERGENiHBG051332.
InParanoidiQ8K301.
KOiK14779.
OMAiNVDCLHA.
OrthoDBiEOG7H1JKD.
TreeFamiTF314448.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
InterProiIPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view]
PfamiPF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view]
SMARTiSM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
PROSITEiPS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8K301-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDSYDLFRRL GAGAKFDVKR FSADATRFQV GKRKFDSESL EVLKGLDFFG
60 70 80 90 100
NKKSVSDECG ALQIHQEPPN EEKTQGVLLE RSKEPKKKKR KKMTSEVPAQ
110 120 130 140 150
EDFDGGIQWT SSVEAKLQDE KVSGEKKLTS GKLEHLRKEK VNFFRNKHKI
160 170 180 190 200
HVQGTDLPDP IATFQQLDQE YKINSRLLQN ILDAGFQVPT PIQMQAIPVM
210 220 230 240 250
LHGRELLASA PTGSGKTLAF SIPILMQLKQ PTNKGFRALV ISPTRELASQ
260 270 280 290 300
IHRELIKISE GTGFRIHMIH KAAIAAKKFG PKSSKKFDIL VTTPNRLIYL
310 320 330 340 350
LKQDPPGIDL TNVEWLVVDE SDKLFEDGKT GFREQLASIF LACTSPKVRR
360 370 380 390 400
AMFSATFAYD VEQWCKLNLD NVVSVSIGAR NSAVETVEQE LLFVGSETGK
410 420 430 440 450
LLAMRELVKK GFKPPVLVFV QSIERAKELF HELIYEGINV DVIHAERTQQ
460 470 480 490 500
QRDNTVHSFR AGKIWVLICT ALLARGIDFK GVNLVINYDF PTSSVEYIHR
510 520 530 540 550
IGRTGRAGNR GKAVTFFTED DKPLLRSVAN VIQQAGCPVP EYIKGFQKLL
560 570 580 590
SKQKKKMIKK PLERESICTT PKYFLEQAKQ KKVAGQNSKK KETLKEKS
Length:598
Mass (Da):67,474
Last modified:July 27, 2011 - v2
Checksum:iB4C89C522C4A79A9
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti75 – 751Q → E in AAH29094. (PubMed:15489334)Curated
Sequence conflicti81 – 811R → K in BAC38014. (PubMed:16141072)Curated
Sequence conflicti103 – 1031F → L in AAH29094. (PubMed:15489334)Curated
Sequence conflicti119 – 1191D → E in AAH29094. (PubMed:15489334)Curated
Sequence conflicti312 – 3121N → S in AAH29094. (PubMed:15489334)Curated
Sequence conflicti373 – 3731V → I in AAH29094. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080767 mRNA. Translation: BAC38014.1.
AK133545 mRNA. Translation: BAE21716.1.
AL645615 Genomic DNA. Translation: CAI25508.1.
CH466556 Genomic DNA. Translation: EDL15728.1.
BC029094 mRNA. Translation: AAH29094.1.
CCDSiCCDS25180.1.
RefSeqiNP_084372.2. NM_030096.2.
UniGeneiMm.280544.

Genome annotation databases

EnsembliENSMUST00000049257; ENSMUSP00000048802; ENSMUSG00000020677.
GeneIDi78394.
KEGGimmu:78394.
UCSCiuc007kpz.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK080767 mRNA. Translation: BAC38014.1 .
AK133545 mRNA. Translation: BAE21716.1 .
AL645615 Genomic DNA. Translation: CAI25508.1 .
CH466556 Genomic DNA. Translation: EDL15728.1 .
BC029094 mRNA. Translation: AAH29094.1 .
CCDSi CCDS25180.1.
RefSeqi NP_084372.2. NM_030096.2.
UniGenei Mm.280544.

3D structure databases

ProteinModelPortali Q8K301.
SMRi Q8K301. Positions 140-544.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 219368. 1 interaction.
STRINGi 10090.ENSMUSP00000048802.

PTM databases

PhosphoSitei Q8K301.

Proteomic databases

MaxQBi Q8K301.
PaxDbi Q8K301.
PRIDEi Q8K301.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000049257 ; ENSMUSP00000048802 ; ENSMUSG00000020677 .
GeneIDi 78394.
KEGGi mmu:78394.
UCSCi uc007kpz.2. mouse.

Organism-specific databases

CTDi 11056.
MGIi MGI:1925644. Ddx52.

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00550000074863.
HOGENOMi HOG000242486.
HOVERGENi HBG051332.
InParanoidi Q8K301.
KOi K14779.
OMAi NVDCLHA.
OrthoDBi EOG7H1JKD.
TreeFami TF314448.

Miscellaneous databases

ChiTaRSi Ddx52. mouse.
NextBioi 348796.
PROi Q8K301.
SOURCEi Search...

Gene expression databases

Bgeei Q8K301.
CleanExi MM_DDX52.
ExpressionAtlasi Q8K301. baseline and differential.
Genevestigatori Q8K301.

Family and domain databases

Gene3Di 3.40.50.300. 2 hits.
InterProi IPR011545. DEAD/DEAH_box_helicase_dom.
IPR014001. Helicase_ATP-bd.
IPR001650. Helicase_C.
IPR027417. P-loop_NTPase.
IPR014014. RNA_helicase_DEAD_Q_motif.
[Graphical view ]
Pfami PF00270. DEAD. 1 hit.
PF00271. Helicase_C. 1 hit.
[Graphical view ]
SMARTi SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view ]
SUPFAMi SSF52540. SSF52540. 1 hit.
PROSITEi PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
PS51195. Q_MOTIF. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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: Retina and Xiphoid cartilage.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Mammary tumor.

Entry informationi

Entry nameiDDX52_MOUSE
AccessioniPrimary (citable) accession number: Q8K301
Secondary accession number(s): Q3UZY9, Q8BV29
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 9, 2003
Last sequence update: July 27, 2011
Last modified: November 26, 2014
This is version 99 of the entry and version 2 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