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Protein

ATP-dependent RNA helicase DDX51

Gene

Ddx51

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

Functioni

ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi228 – 2358ATPPROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX51 (EC:3.6.4.13)
Alternative name(s):
DEAD box protein 51
Gene namesi
Name:Ddx51
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 5

Organism-specific databases

MGIiMGI:1916913. Ddx51.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 639638ATP-dependent RNA helicase DDX51PRO_0000228097Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei79 – 791PhosphoserineCombined sources
Modified residuei432 – 4321PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ6P9R1.
MaxQBiQ6P9R1.
PaxDbiQ6P9R1.
PRIDEiQ6P9R1.

PTM databases

iPTMnetiQ6P9R1.
PhosphoSiteiQ6P9R1.

Expressioni

Gene expression databases

BgeeiQ6P9R1.
CleanExiMM_DDX51.
ExpressionAtlasiQ6P9R1. baseline and differential.
GenevisibleiQ6P9R1. MM.

Interactioni

Protein-protein interaction databases

BioGridi213598. 2 interactions.
STRINGi10090.ENSMUSP00000031478.

Structurei

3D structure databases

ProteinModelPortaliQ6P9R1.
SMRiQ6P9R1. Positions 136-623.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini215 – 424210Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini467 – 615149Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi193 – 2019Q motif
Motifi343 – 3464DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi27 – 9266Arg-richAdd
BLAST

Domaini

The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0350. Eukaryota.
ENOG410XRWM. LUCA.
GeneTreeiENSGT00550000075141.
HOGENOMiHOG000239572.
HOVERGENiHBG081427.
InParanoidiQ6P9R1.
KOiK14807.
OMAiDVPGIHP.
OrthoDBiEOG708VZB.
PhylomeDBiQ6P9R1.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
[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. 3 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q6P9R1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALFHIARYA GPEAAGQGDT DAEAGSRARV LLERLQNRAR ERQQREPELE
60 70 80 90 100
TTGTAGEGEA AAAGKRRRRP RRRRRVSGSA TPNSEAPRAK RRKADKDVDA
110 120 130 140 150
GRGEEAPEEL SAGAEDPGAN PQEDVQRPPA PGRVLGDFAR RKTPKVQPFL
160 170 180 190 200
PAWLAKPSCV KKSVTEDLTP IEDIPEVHPD LQKQLRANGI TSYFPVQAAV
210 220 230 240 250
IPALLESADH GFLIGRGGYQ PSDLCVSAPT GSGKTLAFVI PVVQALLHRV
260 270 280 290 300
VCHIRALVVL PTKELAQQVS KVFNIYTDTT PLRVALVTGQ KSLAKEQESL
310 320 330 340 350
VQKTADGFRC LADIVVATPG RLVDHIDQTP GFSLQQLRFL IIDEADRMID
360 370 380 390 400
SMHQSWLPRV VAAAFYSEGP TGSCALLQRT QPQALTAAST CVPQMPLQKL
410 420 430 440 450
LFSATLTQDP EKLQRLGLYQ PRLFSTRLGQ QSPKDTAEVD ENSGKYTFPV
460 470 480 490 500
GLTHHYVPCR LSSKPLIVLH LVLRMSCSRA LCFTNSRENS HRLYLLAQAF
510 520 530 540 550
GGVSVAEFSS RYGPGQRKKI LKQFEQGKIQ LLISTDATAR GIDVQGVELV
560 570 580 590 600
INYDAPQYLR TYVHRVGRTA RAGKTGQAFT LLLKVQERKF LQMVSEAGVP
610 620 630
ELTHHEIPRK LLQPLVARYE TALSQLEKTV KEEQKLKAA
Length:639
Mass (Da):70,368
Last modified:July 5, 2004 - v1
Checksum:i44127413841C6AAB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti639 – 6391A → D in BAE31347 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK152599 mRNA. Translation: BAE31347.1.
BC060646 mRNA. Translation: AAH60646.1.
CCDSiCCDS19528.1.
RefSeqiNP_081432.2. NM_027156.3.
UniGeneiMm.392735.
Mm.5267.

Genome annotation databases

EnsembliENSMUST00000031478; ENSMUSP00000031478; ENSMUSG00000029504.
GeneIDi69663.
KEGGimmu:69663.
UCSCiuc008yre.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK152599 mRNA. Translation: BAE31347.1.
BC060646 mRNA. Translation: AAH60646.1.
CCDSiCCDS19528.1.
RefSeqiNP_081432.2. NM_027156.3.
UniGeneiMm.392735.
Mm.5267.

3D structure databases

ProteinModelPortaliQ6P9R1.
SMRiQ6P9R1. Positions 136-623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213598. 2 interactions.
STRINGi10090.ENSMUSP00000031478.

PTM databases

iPTMnetiQ6P9R1.
PhosphoSiteiQ6P9R1.

Proteomic databases

EPDiQ6P9R1.
MaxQBiQ6P9R1.
PaxDbiQ6P9R1.
PRIDEiQ6P9R1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000031478; ENSMUSP00000031478; ENSMUSG00000029504.
GeneIDi69663.
KEGGimmu:69663.
UCSCiuc008yre.2. mouse.

Organism-specific databases

CTDi317781.
MGIiMGI:1916913. Ddx51.

Phylogenomic databases

eggNOGiKOG0350. Eukaryota.
ENOG410XRWM. LUCA.
GeneTreeiENSGT00550000075141.
HOGENOMiHOG000239572.
HOVERGENiHBG081427.
InParanoidiQ6P9R1.
KOiK14807.
OMAiDVPGIHP.
OrthoDBiEOG708VZB.
PhylomeDBiQ6P9R1.

Miscellaneous databases

ChiTaRSiDdx51. mouse.
PROiQ6P9R1.
SOURCEiSearch...

Gene expression databases

BgeeiQ6P9R1.
CleanExiMM_DDX51.
ExpressionAtlasiQ6P9R1. baseline and differential.
GenevisibleiQ6P9R1. MM.

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.
IPR000629. RNA-helicase_DEAD-box_CS.
[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. 3 hits.
PROSITEiPS00039. DEAD_ATP_HELICASE. 1 hit.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: Bone marrow.
  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].
    Strain: C57BL/6J.
    Tissue: Brain.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-432, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Spleen and Testis.

Entry informationi

Entry nameiDDX51_MOUSE
AccessioniPrimary (citable) accession number: Q6P9R1
Secondary accession number(s): Q3U7M2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 21, 2006
Last sequence update: July 5, 2004
Last modified: June 8, 2016
This is version 99 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

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 one 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.