UniProt functional annotation for P20449



	UniProt functional annotation for P20449

UniProt code: P20449.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).

Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.

Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription. {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:11350039, ECO:0000269|PubMed:12192043, ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15280434, ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606, ECO:0000269|PubMed:9564047, ECO:0000269|PubMed:9564048}.

Catalytic activity: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;

Subunit: Associates with the nuclear pore complex. Interacts with NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary for the association to the nuclear pore complex. Interacts also with the TFIIH complex subunits TFB1, TFB2 and RAD3. {ECO:0000269|PubMed:10428971, ECO:0000269|PubMed:10523319, ECO:0000269|PubMed:10610322, ECO:0000269|PubMed:12686617, ECO:0000269|PubMed:15574330, ECO:0000269|PubMed:15619606}.

Subcellular location: Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress.

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

Miscellaneous: Present with 14900 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Similarity: Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy:		Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.



Function:		ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription. {ECO:0000269\|PubMed:10428971, ECO:0000269\|PubMed:10523319, ECO:0000269\|PubMed:10610322, ECO:0000269\|PubMed:11350039, ECO:0000269\|PubMed:12192043, ECO:0000269\|PubMed:12686617, ECO:0000269\|PubMed:15280434, ECO:0000269\|PubMed:15574330, ECO:0000269\|PubMed:15619606, ECO:0000269\|PubMed:9564047, ECO:0000269\|PubMed:9564048}.


Catalytic activity:		Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13;
Subunit:		Associates with the nuclear pore complex. Interacts with NUP159, GLE1, GFD1 and ZDS1. The interaction with NUP159 is necessary for the association to the nuclear pore complex. Interacts also with the TFIIH complex subunits TFB1, TFB2 and RAD3. {ECO:0000269\|PubMed:10428971, ECO:0000269\|PubMed:10523319, ECO:0000269\|PubMed:10610322, ECO:0000269\|PubMed:12686617, ECO:0000269\|PubMed:15574330, ECO:0000269\|PubMed:15619606}.
Subcellular location:		Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress.
Domain:		The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Miscellaneous:		Present with 14900 molecules/cell in log phase SD medium. {ECO:0000269\|PubMed:14562106}.
Similarity:		Belongs to the DEAD box helicase family. DDX19/DBP5 subfamily. {ECO:0000305}.