HCSGD entry for PNPT1
1. General information
Official gene symbol | PNPT1 |
---|---|
Entrez ID | 87178 |
Gene full name | polyribonucleotide nucleotidyltransferase 1 |
Other gene symbols | COXPD13 DFNB70 OLD35 PNPASE old-35 |
Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network

This gene isn't in Literature mining network.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
---|---|---|---|
GO:0000175 | 3'-5'-exoribonuclease activity | IDA IEA | molecular_function |
GO:0000957 | Mitochondrial RNA catabolic process | IDA | biological_process |
GO:0000958 | Mitochondrial mRNA catabolic process | IDA | biological_process |
GO:0000962 | Positive regulation of mitochondrial RNA catabolic process | IDA | biological_process |
GO:0000964 | Mitochondrial RNA 5'-end processing | IMP | biological_process |
GO:0000965 | Mitochondrial RNA 3'-end processing | IMP | biological_process |
GO:0003723 | RNA binding | IEA | molecular_function |
GO:0004654 | Polyribonucleotide nucleotidyltransferase activity | IDA IEA | molecular_function |
GO:0005515 | Protein binding | IPI | molecular_function |
GO:0005737 | Cytoplasm | IDA | cellular_component |
GO:0005739 | Mitochondrion | IDA | cellular_component |
GO:0005758 | Mitochondrial intermembrane space | IDA | cellular_component |
GO:0005886 | Plasma membrane | IDA | cellular_component |
GO:0006396 | RNA processing | IEA | biological_process |
GO:0006401 | RNA catabolic process | IDA | biological_process |
GO:0006402 | MRNA catabolic process | IDA IEA | biological_process |
GO:0008266 | Poly(U) RNA binding | IDA | molecular_function |
GO:0034046 | Poly(G) binding | IDA | molecular_function |
GO:0034599 | Cellular response to oxidative stress | IDA | biological_process |
GO:0035198 | MiRNA binding | IDA | molecular_function |
GO:0035458 | Cellular response to interferon-beta | IDA | biological_process |
GO:0035927 | RNA import into mitochondrion | IDA | biological_process |
GO:0035928 | RRNA import into mitochondrion | IDA | biological_process |
GO:0043457 | Regulation of cellular respiration | ISS | biological_process |
GO:0043631 | RNA polyadenylation | IDA | biological_process |
GO:0045025 | Mitochondrial degradosome | IDA | cellular_component |
GO:0045926 | Negative regulation of growth | IDA | biological_process |
GO:0051260 | Protein homooligomerization | IDA | biological_process |
GO:0061014 | Positive regulation of mRNA catabolic process | IMP | biological_process |
GO:0070207 | Protein homotrimerization | IDA | biological_process |
GO:0070584 | Mitochondrion morphogenesis | ISS | biological_process |
GO:0071042 | Nuclear polyadenylation-dependent mRNA catabolic process | IDA | biological_process |
GO:0071850 | Mitotic cell cycle arrest | IDA | biological_process |
GO:0090305 | Nucleic acid phosphodiester bond hydrolysis | IDA | biological_process |
GO:0090501 | RNA phosphodiester bond hydrolysis | IDA | biological_process |
GO:0090503 | RNA phosphodiester bond hydrolysis, exonucleolytic | IDA | biological_process |
GO:0097222 | Mitochondrial mRNA polyadenylation | IMP | biological_process |
GO:2000627 | Positive regulation of miRNA catabolic process | IDA | biological_process |
GO:2000772 | Regulation of cellular senescence | IDA | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
p-value up | p-value down | FDR up | FDR down |
---|---|---|---|
0.2928862543 | 0.0795313058 | 0.9931794769 | 0.5326573791 |
- Individual experiment result
( "-" represent NA in the specific microarray platform )
( "-" represent NA in the specific microarray platform )
Data source | Up or down | Log fold change |
---|---|---|
GSE11954 | Up | 0.2018065115 |
GSE13712_SHEAR | Up | 0.8713290641 |
GSE13712_STATIC | Up | 0.8139471474 |
GSE19018 | Down | -0.6225162056 |
GSE19899_A1 | Up | 0.1236508630 |
GSE19899_A2 | Down | -0.1787222591 |
PubMed_21979375_A1 | Up | 0.8097809438 |
PubMed_21979375_A2 | Up | 0.1013526789 |
GSE35957 | Down | -0.9029902167 |
GSE36640 | Down | -0.9790038704 |
GSE54402 | Up | 0.2408254901 |
GSE9593 | Down | -0.6230177007 |
GSE43922 | Up | 0.0075517089 |
GSE24585 | Down | -0.7032014102 |
GSE37065 | Up | 0.7778881346 |
GSE28863_A1 | - | - |
GSE28863_A2 | - | - |
GSE28863_A3 | - | - |
GSE28863_A4 | - | - |
GSE48662 | Down | -0.3631011986 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
---|---|---|---|---|---|
hsa-miR-155-5p | MIMAT0000646 | MIRT020848 | Proteomics | Functional MTI (Weak) | 18668040 |
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- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 11 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
---|---|
22370639 | The tumor-suppressive effect of ZNF331 is mediated at least by downregulation of genes involved in cell growth promotion (DSTN, EIF5A, GARS, DDX5, STAM, UQCRFS1 and SET) and migration/invasion (DSTN and ACTR3), and upregulation of genome-stability gene (SSBP1) and cellular senescence gene (PNPT1) |
22210891 | Crystal structure of human polynucleotide phosphorylase: insights into its domain function in RNA binding and degradation |
22210891 | Human polynucleotide phosphorylase (hPNPase) is a 3'-to-5' exoribonuclease that degrades specific mRNA and miRNA, and imports RNA into mitochondria, and thus regulates diverse physiological processes, including cellular senescence and homeostasis |
22210891 | However, the RNA-processing mechanism by hPNPase, particularly how RNA is bound via its various domains, remains obscure |
22210891 | Here, we report the crystal structure of an S1 domain-truncated hPNPase at a resolution of 2 |
22210891 | The trimeric hPNPase has a hexameric ring-like structure formed by six RNase PH domains, capped with a trimeric KH pore |
22210891 | Our biochemical and mutagenesis studies suggest that the S1 domain is not critical for RNA binding, and conversely, that the conserved GXXG motif in the KH domain directly participates in RNA binding in hPNPase |
22210891 | Our studies thus provide structural and functional insights into hPNPase, which uses a KH pore to trap a long RNA 3' tail that is further delivered into an RNase PH channel for the degradation process |
22210891 | Structural RNA with short 3' tails are, on the other hand, transported but not digested by hPNPase |
18678873 | In yeast mitochondria, RNA degradation takes place through the coordinated activities of ySuv3 helicase and yDss1 exoribonuclease (mtEXO), whereas in bacteria, RNA is degraded via RNaseE, RhlB, PNPase, and enolase |
17983748 | Human polynucleotide phosphorylase: location matters |
17983748 | Human polynucleotide phosphorylase (hPNPase) is an RNA-processing enzyme induced in response to type I interferons and during terminal differentiation and cellular senescence |
17983748 | Initial studies have also linked hPNPase to tumorigenesis and the cellular response to viral infection |
17983748 | Its surprising localization in the IMS, which is thought to be devoid of mRNA transcripts, raises questions about where and how hPNPase elicits its numerous suggested functions |
17983748 | Here, we discuss recent advances in understanding the various roles of hPNPase both within and potentially outside of the mitochondria |
16505900 | Up-regulation of human PNPase mRNA by beta-interferon has no effect on protein level in melanoma cell lines |
16505900 | Human mitochondrial polynucleotide phosphorylase (hPNPase) is an exoribonuclease localized in mitochondria |
16505900 | Recent studies have revealed the existence of a relationship between induction of hPNPase mRNA and both cellular senescence and growth arrest of melanoma cells following beta-interferon treatment |
16505900 | The aim of this study was to verify whether the augmented hPNPase mRNA level results in increase of the protein level |
16505900 | However, an elevated level of hPNPase protein was observed in interferon-induced HeLa and Jurkat cells |
16055741 | Human polynucleotide phosphorylase (hPNPase(OLD-35)), an evolutionarily conserved 3', 5' exoribonuclease mediating mRNA degradation, was first identified as a predominantly mitochondrial protein overexpressed during terminal differentiation and senescence |
15978720 | Human polynucleotide phosphorylase (hPNPase(old-35)), a RNA degradation enzyme shown to be upregulated during differentiation and cellular senescence, may represent a molecular link between aging and its associated inflammation |
15492272 | Human polynucleotide phosphorylase (hPNPaseold-35): a potential link between aging and inflammation |
15492272 | An overlapping pathway screen identified human polynucleotide phosphorylase (hPNPase(old-35)), an evolutionary conserved 3',5'-exoribonuclease, as a gene up-regulated during both terminal differentiation and cellular senescence |
14563561 | Expression regulation and genomic organization of human polynucleotide phosphorylase, hPNPase(old-35), a Type I interferon inducible early response gene |
14563561 | Sequence and functional analysis indicates that old-35 encodes human polynucleotide phosphorylase, hPNPase(old-35) |
14563561 | To provide insights into PNPase function in vivo, we have also cloned the mouse PNPase(old-35) cDNA, mPNPase(old-35) |
12798676 | Human polynucleotide phosphorylase, hPNPase, is localized in mitochondria |
12798676 | The human gene encoding a polynucleotide phosphorylase (hPNPase) has been recently identified as strongly up-regulated in two processes leading to irreversible arrest of cell division: progeroid senescence and terminal differentiation |
12798676 | Here, we demonstrate that the hPNPase is localized in mitochondria |
12473748 | Identification and cloning of human polynucleotide phosphorylase, hPNPase old-35, in the context of terminal differentiation and cellular senescence |
12473748 | This strategy identified old-35, which encodes an evolutionary conserved gene, human polynucleotide phosphorylase (hPNPase(old-35)), that is regulated predominantly by type I IFNs |
12473748 | Identification of hPNPase(old-35), an IFN-inducible 3'-5' RNA exonuclease, provides additional support for a relationship between IFN action and RNA processing and suggests an important role for this gene in growth control associated with terminal differentiation and cellular senescence |
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