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Q61655

- DD19A_MOUSE

UniProt

Q61655 - DD19A_MOUSE

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Protein

ATP-dependent RNA helicase DDX19A

Gene

Ddx19a

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei118 – 1181ATPBy similarity
Binding sitei428 – 4281ATPBy similarity
Binding sitei431 – 4311ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi137 – 1448ATPPROSITE-ProRule annotation

GO - Molecular functioni

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

GO - Biological processi

  1. mRNA transport Source: UniProtKB-KW
  2. positive regulation of apoptotic process Source: Ensembl
  3. protein transport Source: UniProtKB-KW
  4. response to zinc ion Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

mRNA transport, Protein transport, Translocation, Transport

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:99526. Ddx19a.

Subcellular locationi

Cytoplasm By similarity. Nucleusnuclear pore complex. Nucleus membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Nuclear pore complex cytoplasmic fibrils.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-KW
  2. nuclear pore Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nuclear pore complex, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 478477ATP-dependent RNA helicase DDX19APRO_0000055023Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ61655.
PaxDbiQ61655.
PRIDEiQ61655.

2D gel databases

REPRODUCTION-2DPAGEQ61655.

PTM databases

PhosphoSiteiQ61655.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiQ61655.
CleanExiMM_DDX19A.
GenevestigatoriQ61655.

Interactioni

Protein-protein interaction databases

BioGridi199417. 2 interactions.
IntActiQ61655. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ61655.
SMRiQ61655. Positions 59-466.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini124 – 294171Helicase ATP-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini305 – 473169Helicase C-terminalPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 299298N-terminal lobeBy similarityAdd
BLAST
Regioni54 – 6714N-terminal helixBy similarityAdd
BLAST
Regioni300 – 478179C-terminal lobeBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi91 – 11929Q motifAdd
BLAST
Motifi241 – 2444DEAD box

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi48 – 536Poly-Glu

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

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

Phylogenomic databases

eggNOGiCOG0513.
GeneTreeiENSGT00530000063236.
HOGENOMiHOG000268797.
HOVERGENiHBG107989.
InParanoidiQ61655.
OMAiMMAINTI.
OrthoDBiEOG7TMZRJ.
TreeFamiTF314957.

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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 323VKA → AKS in AAA53629. (PubMed:8144024)Curated
Sequence conflicti262 – 2632ML → IV in AAA53629. (PubMed:8144024)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS22668.1.
PIRi I49731.
RefSeqi NP_031942.2. NM_007916.2.
UniGenei Mm.287901.

3D structure databases

ProteinModelPortali Q61655.
SMRi Q61655. Positions 59-466.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199417. 2 interactions.
IntActi Q61655. 1 interaction.

PTM databases

PhosphoSitei Q61655.

2D gel databases

REPRODUCTION-2DPAGE Q61655.

Proteomic databases

MaxQBi Q61655.
PaxDbi Q61655.
PRIDEi Q61655.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000040416 ; ENSMUSP00000047898 ; ENSMUSG00000015023 .
GeneIDi 13680.
KEGGi mmu:13680.
UCSCi uc009nll.2. mouse.

Organism-specific databases

CTDi 55308.
MGIi MGI:99526. Ddx19a.

Phylogenomic databases

eggNOGi COG0513.
GeneTreei ENSGT00530000063236.
HOGENOMi HOG000268797.
HOVERGENi HBG107989.
InParanoidi Q61655.
OMAi MMAINTI.
OrthoDBi EOG7TMZRJ.
TreeFami TF314957.

Miscellaneous databases

ChiTaRSi DDX19A. mouse.
NextBioi 284434.
PROi Q61655.
SOURCEi Search...

Gene expression databases

Bgeei Q61655.
CleanExi MM_DDX19A.
Genevestigatori Q61655.

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

« Hide 'large scale' publications
  1. "Mouse erythroid cells express multiple putative RNA helicase genes exhibiting high sequence conservation from yeast to mammals."
    Gee S.L., Conboy J.G.
    Gene 140:171-177(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Erythroleukemia.
  2. "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 and Stomach.
  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].

Entry informationi

Entry nameiDD19A_MOUSE
AccessioniPrimary (citable) accession number: Q61655
Secondary accession number(s): Q543M2, Q921R0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 132 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. 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

External Data

Dasty 3