#ID(s) interactor A	ID(s) interactor B	Alt. ID(s) interactor A	Alt. ID(s) interactor B	Alias(es) interactor A	Alias(es) interactor B	Interaction detection method(s)	Publication 1st author(s)	Publication Identifier(s)	Taxid interactor A	Taxid interactor B	Interaction type(s)	Source database(s)	Interaction identifier(s)	Confidence value(s)	Expansion method(s)	Biological role(s) interactor A	Biological role(s) interactor B	Experimental role(s) interactor A	Experimental role(s) interactor B	Type(s) interactor A	Type(s) interactor B	Xref(s) interactor A	Xref(s) interactor B	Interaction Xref(s)	Annotation(s) interactor A	Annotation(s) interactor B	Interaction annotation(s)	Host organism(s)	Interaction parameter(s)	Creation date	Update date	Checksum(s) interactor A	Checksum(s) interactor B	Interaction Checksum(s)	Negative	Feature(s) interactor A	Feature(s) interactor B	Stoichiometry(s) interactor A	Stoichiometry(s) interactor B	Identification method participant A	Identification method participant B
uniprotkb:Q8VDG3	uniprotkb:Q8VDG3	intact:EBI-8402250|intact:MINT-4106622|uniprotkb:Q8C7N6|uniprotkb:Q9DC46	intact:EBI-8402250|intact:MINT-4106622|uniprotkb:Q8C7N6|uniprotkb:Q9DC46	psi-mi:parn_mouse(display_long)|uniprotkb:Parn(gene name)|psi-mi:Parn(display_short)|uniprotkb:Polyadenylate-specific ribonuclease(gene name synonym)	psi-mi:parn_mouse(display_long)|uniprotkb:Parn(gene name)|psi-mi:Parn(display_short)|uniprotkb:Polyadenylate-specific ribonuclease(gene name synonym)	psi-mi:"MI:0114"(x-ray crystallography)	Wu et al. (2009)	pubmed:19217398|doi:10.1016/j.str.2008.11.012|imex:IM-11788	taxid:10090(mouse)|taxid:10090(Mus musculus)	taxid:10090(mouse)|taxid:10090(Mus musculus)	psi-mi:"MI:0407"(direct interaction)	psi-mi:"MI:0465"(DIP)	intact:EBI-15757471|imex:IM-11788-1|dip:DIP-102562E	-	-	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0499"(unspecified role)	psi-mi:"MI:0326"(protein)	psi-mi:"MI:0326"(protein)	refseq:NP_083037.1|dip:DIP-48330N|mint:Q8VDG3|go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0000184"(nuclear-transcribed mRNA catabolic process, nonsense-mediated decay)|go:"GO:0000289"("nuclear-transcribed mRNA poly(A) tail shortening")|go:"GO:0000495"(box H/ACA RNA 3'-end processing)|go:"GO:0003723"(RNA binding)|go:"GO:0004535"("poly(A)-specific ribonuclease activity")|go:"GO:0005730"(nucleolus)|go:"GO:0005737"(cytoplasm)|go:"GO:0010587"(miRNA catabolic process)|go:"GO:0016607"(nuclear speck)|go:"GO:0019901"(protein kinase binding)|go:"GO:0032212"(positive regulation of telomere maintenance via telomerase)|go:"GO:0043169"(cation binding)|go:"GO:0046872"(metal ion binding)|go:"GO:0051973"(positive regulation of telomerase activity)|go:"GO:0071051"(polyadenylation-dependent snoRNA 3'-end processing)|go:"GO:0090503"(RNA phosphodiester bond hydrolysis, exonucleolytic)|go:"GO:0090669"(telomerase RNA stabilization)|go:"GO:0110008"(ncRNA deadenylation)|go:"GO:1904872"(regulation of telomerase RNA localization to Cajal body)|interpro:IPR001374(Single-stranded nucleic acid binding R3H)|interpro:IPR006941(Ribonuclease CAF1)|interpro:IPR012337(Polynucleotidyl transferase, Ribonuclease H fold)|interpro:IPR012677(Nucleotide-binding, alpha-beta plait)|interpro:IPR014789("Poly(A)-specific ribonuclease, RNA binding")|interpro:IPR034042|interpro:IPR035979|interpro:IPR036397|interpro:IPR036867|rcsb pdb:1UG8|rcsb pdb:1WHV|rcsb pdb:2ROK|rcsb pdb:3D45|reactome:R-MMU-429947|reactome:R-MMU-450604	refseq:NP_083037.1|dip:DIP-48330N|mint:Q8VDG3|go:"GO:0000175"(3'-5'-exoribonuclease activity)|go:"GO:0000184"(nuclear-transcribed mRNA catabolic process, nonsense-mediated decay)|go:"GO:0000289"("nuclear-transcribed mRNA poly(A) tail shortening")|go:"GO:0000495"(box H/ACA RNA 3'-end processing)|go:"GO:0003723"(RNA binding)|go:"GO:0004535"("poly(A)-specific ribonuclease activity")|go:"GO:0005730"(nucleolus)|go:"GO:0005737"(cytoplasm)|go:"GO:0010587"(miRNA catabolic process)|go:"GO:0016607"(nuclear speck)|go:"GO:0019901"(protein kinase binding)|go:"GO:0032212"(positive regulation of telomere maintenance via telomerase)|go:"GO:0043169"(cation binding)|go:"GO:0046872"(metal ion binding)|go:"GO:0051973"(positive regulation of telomerase activity)|go:"GO:0071051"(polyadenylation-dependent snoRNA 3'-end processing)|go:"GO:0090503"(RNA phosphodiester bond hydrolysis, exonucleolytic)|go:"GO:0090669"(telomerase RNA stabilization)|go:"GO:0110008"(ncRNA deadenylation)|go:"GO:1904872"(regulation of telomerase RNA localization to Cajal body)|interpro:IPR001374(Single-stranded nucleic acid binding R3H)|interpro:IPR006941(Ribonuclease CAF1)|interpro:IPR012337(Polynucleotidyl transferase, Ribonuclease H fold)|interpro:IPR012677(Nucleotide-binding, alpha-beta plait)|interpro:IPR014789("Poly(A)-specific ribonuclease, RNA binding")|interpro:IPR034042|interpro:IPR035979|interpro:IPR036397|interpro:IPR036867|rcsb pdb:1UG8|rcsb pdb:1WHV|rcsb pdb:2ROK|rcsb pdb:3D45|reactome:R-MMU-429947|reactome:R-MMU-450604	psi-mi:"MI:0465"(dip)	comment:mint|function:"3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization"	comment:mint|function:"3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization"	full coverage:Only protein-protein interactions|curation depth:imex curation	taxid:562(ecolx)|taxid:562(Escherichia coli)	-	2017/08/06	2017/08/10	rogid:X82UAPZBe5zWu+3h3nFrZocZQFs10090	rogid:X82UAPZBe5zWu+3h3nFrZocZQFs10090	rigid:EaquMOJzJ7qHccn/7Cs03o/eVm8	false	binding-associated region:1-510	binding-associated region:1-510	-	0	psi-mi:"MI:0396"(predetermined participant)	psi-mi:"MI:0396"(predetermined participant)