Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

Annotation inferences using phylogenetic trees

Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt

Gene Ontology annotation based on curation of immunofluorescence data

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

Down-regulation of Myc as a potential target for growth arrest induced by human polynucleotide phosphorylase (hPNPaseold-35) in human melanoma cells.

Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria.

Defining the domains of human polynucleotide phosphorylase (hPNPaseOLD-35) mediating cellular senescence.

Defining the mechanism by which IFN-beta dowregulates c-myc expression in human melanoma cells: pivotal role for human polynucleotide phosphorylase (hPNPaseold-35).

The TCL1 oncoprotein binds the RNase PH domains of the PNPase exoribonuclease without affecting its RNA degrading activity.

Mammalian polynucleotide phosphorylase is an intermembrane space RNase that maintains mitochondrial homeostasis.

Analysis of the human polynucleotide phosphorylase (PNPase) reveals differences in RNA binding and response to phosphate compared to its bacterial and chloroplast counterparts.

Stable PNPase RNAi silencing: its effect on the processing and adenylation of human mitochondrial RNA.

Human polynucleotide phosphorylase reduces oxidative RNA damage and protects HeLa cell against oxidative stress.

Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality.

Human mitochondrial RNA turnover caught in flagranti: involvement of hSuv3p helicase in RNA surveillance.

Human polynucleotide phosphorylase selectively and preferentially degrades microRNA-221 in human melanoma cells.

PNPASE regulates RNA import into mitochondria.

LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria.

The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts.

Architecture of the human interactome defines protein communities and disease networks.

Dedicated surveillance mechanism controls G-quadruplex forming non-coding RNAs in human mitochondria.

A reference map of the human binary protein interactome.

Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

RNA 5-methylcytosine marks mitochondrial double-stranded RNAs for degradation and cytosolic release.

Systematic identification of post-transcriptional regulatory modules.

Mitochondrial RNA degradation

SUPV3L1:PNPT1 hydrolyzes mitochondrial RNA to yield 4-5 nucleotide oligoribonucleotides

SUPV3L1 unwinds double-stranded mitochondrial RNA

A mutation in PNPT1, encoding mitochondrial-RNA-import protein PNPase, causes hereditary hearing loss.

Mutation in PNPT1, which encodes a polyribonucleotide nucleotidyltransferase, impairs RNA import into mitochondria and causes respiratory-chain deficiency.

Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci.

PNPase knockout results in mtDNA loss and an altered metabolic gene expression program.

Mitochondrial double-stranded RNA triggers antiviral signalling in humans.