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Protein

ATP-dependent RNA helicase DDX19A

Gene

Ddx19a

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

Functioni

ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19 functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins (By similarity).By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei118ATPBy similarity1
Binding sitei428ATPBy similarity1
Binding sitei431ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi137 – 144ATPPROSITE-ProRule annotation8

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHelicase, Hydrolase, RNA-binding
Biological processmRNA transport, Protein transport, Translocation, Transport
LigandATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
ATP-dependent RNA helicase DDX19A (EC:3.6.4.13)
Alternative name(s):
DEAD box RNA helicase DEAD5
Short name:
mDEAD5
DEAD box protein 19A
Eukaryotic translation initiation factor 4A-related sequence 1
Gene namesi
Name:Ddx19a
Synonyms:Ddx19, Eif4a-rs1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:99526 Ddx19a

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000550232 – 478ATP-dependent RNA helicase DDX19AAdd BLAST477

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Cross-linki26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki26Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei42PhosphothreonineBy similarity1

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ61655
MaxQBiQ61655
PaxDbiQ61655
PeptideAtlasiQ61655
PRIDEiQ61655

2D gel databases

REPRODUCTION-2DPAGEiQ61655

PTM databases

iPTMnetiQ61655
PhosphoSitePlusiQ61655
SwissPalmiQ61655

Expressioni

Tissue specificityi

Found in testis, heart, brain, liver, skeletal muscle, and kidney.

Gene expression databases

BgeeiENSMUSG00000015023
CleanExiMM_DDX19A
GenevisibleiQ61655 MM

Interactioni

Protein-protein interaction databases

BioGridi199417, 3 interactors
IntActiQ61655, 1 interactor
STRINGi10090.ENSMUSP00000047898

Structurei

3D structure databases

ProteinModelPortaliQ61655
SMRiQ61655
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini124 – 294Helicase ATP-bindingPROSITE-ProRule annotationAdd BLAST171
Domaini305 – 473Helicase C-terminalPROSITE-ProRule annotationAdd BLAST169

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni2 – 299N-terminal lobeBy similarityAdd BLAST298
Regioni54 – 67N-terminal helixBy similarityAdd BLAST14
Regioni300 – 478C-terminal lobeBy similarityAdd BLAST179

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi91 – 119Q motifAdd BLAST29
Motifi241 – 244DEAD box4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi48 – 53Poly-Glu6

Domaini

The N-terminal extension helix acts as an autoinhibitory domain, preventing ATP hydrolysis, unless the N-terminus of the protein is displaced by RNA binding, allowing cleft closure to bring key side chains into position for catalysis.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0332 Eukaryota
ENOG410XRGX LUCA
GeneTreeiENSGT00530000063236
HOGENOMiHOG000268797
HOVERGENiHBG107989
InParanoidiQ61655
KOiK18655
OMAiDFKNLCM
OrthoDBiEOG091G03PS
TreeFamiTF314957

Family and domain databases

CDDicd00079 HELICc, 1 hit
InterProiView protein in InterPro
IPR011545 DEAD/DEAH_box_helicase_dom
IPR014001 Helicase_ATP-bd
IPR001650 Helicase_C
IPR027417 P-loop_NTPase
IPR014014 RNA_helicase_DEAD_Q_motif
PfamiView protein in Pfam
PF00270 DEAD, 1 hit
PF00271 Helicase_C, 1 hit
SMARTiView protein in SMART
SM00487 DEXDc, 1 hit
SM00490 HELICc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
PROSITEiView protein in PROSITE
PS51192 HELICASE_ATP_BIND_1, 1 hit
PS51194 HELICASE_CTER, 1 hit
PS51195 Q_MOTIF, 1 hit

Sequencei

Sequence statusi: Complete.

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

Q61655-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATDSWALAV DEQEAAVKSM SSLQIKEEKV KADTNGVIKT STTAEKTEEE
60 70 80 90 100
EKEDRAAQSL LNKLIRSNLV DNTNQVEVLQ RDPSSPLYSV KSFEELRLKP
110 120 130 140 150
QLLQGVYAMG FNRPSKIQEN ALPMMLAEPP QNLIAQSQSG TGKTAAFVLA
160 170 180 190 200
MLSRVEPADR YPQCLCLSPT YELALQTGKV IEQMGKFHPE LKLAYAVRGN
210 220 230 240 250
KLERGQKVSE QIVIGTPGTV LDWCSKLKFI DPKKIKVFVL DEADVMIATQ
260 270 280 290 300
GHQDQSIRIQ RMLPRNCQML LFSATFEDSV WKFAQKVVPD PNIIKLKREE
310 320 330 340 350
ETLDTIKQYY VLCNNREEKF QALCNLYGAI TIAQAMIFCH TRKTASWLAA
360 370 380 390 400
ELSKEGHQVA LLSGEMMVEQ RAAVIERFRE GKEKVLVTTN VCARGIDVEQ
410 420 430 440 450
VSVVINFDLP VDKDGNPDNE TYLHRIGRTG RFGKRGLAVN MVDSKHSMNI
460 470
LNRIQEHFNK KIERLDTDDL DEIEKIAN
Length:478
Mass (Da):53,933
Last modified:July 27, 2011 - v2
Checksum:i46BDE331544EDA7E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti30 – 32VKA → AKS in AAA53629 (PubMed:8144024).Curated3
Sequence conflicti262 – 263ML → IV in AAA53629 (PubMed:8144024).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L25125 mRNA Translation: AAA53629.1
AK049467 mRNA Translation: BAC33762.1
AK146548 mRNA Translation: BAE27252.1
CH466525 Genomic DNA Translation: EDL11480.1
BC011270 mRNA Translation: AAH11270.1
CCDSiCCDS22668.1
PIRiI49731
RefSeqiNP_031942.2, NM_007916.2
UniGeneiMm.287901

Genome annotation databases

EnsembliENSMUST00000040416; ENSMUSP00000047898; ENSMUSG00000015023
GeneIDi13680
KEGGimmu:13680
UCSCiuc009nll.2 mouse

Similar proteinsi

Entry informationi

Entry nameiDD19A_MOUSE
AccessioniPrimary (citable) accession number: Q61655
Secondary accession number(s): Q543M2, Q921R0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: May 23, 2018
This is version 163 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Translation initiation factors
    List of translation initiation factor entries
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

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