HCSGD entry for POMP
1. General information
| Official gene symbol | POMP |
|---|---|
| Entrez ID | 51371 |
| Gene full name | proteasome maturation protein |
| Other gene symbols | C13orf12 PNAS-110 UMP1 |
| 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:0000502 | Proteasome complex | IEA | cellular_component |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005634 | Nucleus | IDA | cellular_component |
| GO:0005730 | Nucleolus | IDA | cellular_component |
| GO:0005783 | Endoplasmic reticulum | IEA | cellular_component |
| GO:0005829 | Cytosol | IEA | cellular_component |
| GO:0031090 | Organelle membrane | IEA | cellular_component |
| GO:0043248 | Proteasome assembly | IMP | biological_process |
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4. Expression levels in datasets
- Meta-analysis result
| p-value up | p-value down | FDR up | FDR down |
|---|---|---|---|
| 0.1650496980 | 0.5841097147 | 0.8034974681 | 1.0000000000 |
- 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 | 0.2208607320 |
| GSE13712_SHEAR | Up | 0.2159386569 |
| GSE13712_STATIC | Up | 0.2240966806 |
| GSE19018 | Down | -0.1751298543 |
| GSE19899_A1 | Up | 0.4140393726 |
| GSE19899_A2 | Up | 0.2048078760 |
| PubMed_21979375_A1 | Down | -0.0926999528 |
| PubMed_21979375_A2 | Up | 0.1322599734 |
| GSE35957 | Up | 0.0535198003 |
| GSE36640 | Up | 0.4148115368 |
| GSE54402 | Up | 0.2529715021 |
| GSE9593 | Up | 0.0433241524 |
| GSE43922 | Down | -0.0361162749 |
| GSE24585 | Down | -0.2801456873 |
| GSE37065 | Up | 0.1545615595 |
| GSE28863_A1 | Down | -0.2309545465 |
| GSE28863_A2 | Down | -0.4679352250 |
| GSE28863_A3 | Down | -0.3351725453 |
| GSE28863_A4 | Up | 0.4234737643 |
| GSE48662 | Down | -0.0832261786 |
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-96-5p | MIMAT0000095 | MIRT027886 | Sequencing | Functional MTI (Weak) | 20371350 |
| hsa-miR-26b-5p | MIMAT0000083 | MIRT028989 | Microarray | Functional MTI (Weak) | 19088304 |
| hsa-miR-301a-3p | MIMAT0000688 | MIRT044227 | CLASH | Functional MTI (Weak) | 23622248 |
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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: 2 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 19467248 | In this study, we have investigated whether proteasome impairment, caused by deletion of UMP1, a gene necessary for the 20S proteasome biogenesis, may influence the stability of the yeast mitochondrial genome |
| 19467248 | Deletion of UMP1 significantly increases also the frequency of respiration-defective mutants having gross rearrangements of the mitochondrial genome |
| 16337885 | Ump1 extends yeast lifespan and enhances viability during oxidative stress: central role for the proteasome |
| 16337885 | In these studies the preservation of proteasome-mediated protein degradation was achieved via increased expression of the proteasome assembly protein Ump1 |
| 16337885 | We observed that Saccharomyces cerevisiae transformed to express increased levels of Ump1 exhibited increased viability in response to a variety of oxidative stressors (menadione, hydrogen peroxide, 4-hydroxynonenal) |
| 16337885 | Interestingly, cells expressing Ump1 were observed to initially have robust elevations in oxidized protein levels following the addition of oxidative stressors, but exhibited a significantly reduced level of oxidized proteins following the removal of oxidative stressors |
| 16337885 | Cells expressing elevated levels of Ump1 also exhibited an enhanced preservation of proteasome-mediated protein degradation, and enhanced viability during stationary-phase aging |
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