Version 5.4
Bos taurus Gene: CPSF4
Summary
InnateDB Gene IDBG-640801.3
Last Modified 2014-10-13 [Report errors or provide feedback]
Gene Symbol CPSF4
Gene Name Cleavage and polyadenylation specificity factor subunit 4
Synonyms NAR
Species Bos taurus
Ensembl Gene ENSBTAG00000002090
Encoded Proteins
IDBP-693101
Cleavage and polyadenylation specificity factor subunit 4
Protein Structure
Useful resources Stemformatics EHFPI ImmGen
Entrez Gene
Summary This gene does not have any Entrez summary - the following is the summary from its human ortholog ENSG00000160917:
Inhibition of the nuclear export of poly(A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. The NS1 effector domain functionally interacts with the cellular 30 kDa subunit of cleavage and polyadenylation specific factor 4, an essential component of the 3' end processing machinery of cellular pre-mRNAs. In influenza virus-infected cells, the NS1 protein is physically associated with cleavage and polyadenylation specific factor 4, 30kD subunit. Binding of the NS1 protein to the 30 kDa protein in vitro prevents CPSF binding to the RNA substrate and inhibits 3' end cleavage and polyadenylation of host pre-mRNAs. Thus the NS1 protein selectively inhibits the nuclear export of cellular, and not viral, mRNAs. Multiple alternatively spliced transcript variants that encode different isoforms have been described for this gene. [provided by RefSeq, Jul 2008]
Inhibition of the nuclear export of poly(A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. The NS1 effector domain functionally interacts with the cellular 30 kDa subunit of cleavage and polyadenylation specific factor 4, an essential component of the 3\' end processing machinery of cellular pre-mRNAs. In influenza virus-infected cells, the NS1 protein is physically associated with cleavage and polyadenylation specific factor 4, 30kD subunit. Binding of the NS1 protein to the 30 kDa protein in vitro prevents CPSF binding to the RNA substrate and inhibits 3\' end cleavage and polyadenylation of host pre-mRNAs. Thus the NS1 protein selectively inhibits the nuclear export of cellular, and not viral, mRNAs. Multiple alternatively spliced transcript variants that encode different isoforms have been described for this gene. [provided by RefSeq, Jul 2008]
Gene Information
Type Protein coding
Genomic Location Chromosome 25:37500102-37512370
Strand Reverse strand
Band
Transcripts
ENSBTAT00000002701 ENSBTAP00000002701
Interactions
Number of Interactions This gene and/or its encoded proteins are associated with 2 experimentally validated interaction(s) in this database.
They are also associated with 9 interaction(s) predicted by orthology.
Experimentally validated
Total 2 [view]
Protein-Protein 2 [view]
Protein-DNA 0
Protein-RNA 0
DNA-DNA 0
RNA-RNA 0
DNA-RNA 0
Predicted by orthology
Total 9 [view]
Gene Ontology

Molecular Function
Accession GO Term
GO:0003676 nucleic acid binding
GO:0003723 RNA binding
GO:0005515 protein binding
GO:0008270 zinc ion binding
GO:0044822 poly(A) RNA binding
GO:0046872 metal ion binding
Biological Process
GO:0006397 mRNA processing
Cellular Component
GO:0005634 nucleus
GO:0005847 mRNA cleavage and polyadenylation specificity factor complex
Orthologs
Species
Homo sapiens
Mus musculus
Gene ID
Gene Order
ENSG00000160917
View Gene Order
ENSMUSG00000029625
View Gene Order
Pathway Predictions based on Human Orthology Data
NETPATH
REACTOME
REACT_6173
Inhibition of Host mRNA Processing and RNA Silencing pathway
REACT_6167
Influenza Infection pathway
REACT_6222
NS1 Mediated Effects on Host Pathways pathway
REACT_6323
Host Interactions with Influenza Factors pathway
REACT_116125
Disease pathway
KEGG
hsa03015
mRNA surveillance pathway pathway
mmu03015
mRNA surveillance pathway pathway
INOH
PID NCI
Cross-References
SwissProt O19137
TrEMBL
UniProt Splice Variant
Entrez Gene 280875
UniGene Bt.55595
RefSeq NM_173942 XM_005225004
HUGO
OMIM
CCDS
HPRD
IMGT
EMBL U96448
GenPept AAC48759
RNA Seq Atlas 280875

If you use InnateDB for your research, please cite the following publication:

Breuer et al., InnateDB: systems biology of innate immunity and beyond - recent updates and continuing curation. Nucl. Acids Res. (2013) 41 (D1) 

InnateDB is being developed jointly by the Brinkman Laboratory (Simon Fraser University, British Columbia, Canada), the Hancock Laboratory (University of British Columbia, Vancouver, British Columbia) and the Lynn EMBL Australia Group (South Australian Health & Medical Research Institute and Flinders University, Adelaide, Australia).

Funding is currently provided by Allergen and EMBL Australia. Previous funding has been provided by Genome Canada, the Foundation for the National Institutes of Health through the Grand Challenges in Global Health initiative and by Teagasc. InnateDB curated interactions are licensed under the Design Science License. All other data is licensed under the terms of the originating database. Contact: innatedb-mail@sfu.ca