HCSGD entry for TGS1
1. General information
Official gene symbol | TGS1 |
---|---|
Entrez ID | 96764 |
Gene full name | trimethylguanosine synthase 1 |
Other gene symbols | NCOA6IP PIMT PIPMT |
Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network

This gene isn't in PPI subnetwork.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
---|---|---|---|
GO:0000387 | Spliceosomal snRNP assembly | TAS | biological_process |
GO:0005515 | Protein binding | IPI | molecular_function |
GO:0005634 | Nucleus | IDA | cellular_component |
GO:0005654 | Nucleoplasm | TAS | cellular_component |
GO:0005737 | Cytoplasm | IDA | cellular_component |
GO:0005829 | Cytosol | TAS | cellular_component |
GO:0006351 | Transcription, DNA-templated | IEA | biological_process |
GO:0006355 | Regulation of transcription, DNA-templated | IEA | biological_process |
GO:0009452 | 7-methylguanosine RNA capping | IEA | biological_process |
GO:0010467 | Gene expression | TAS | biological_process |
GO:0015030 | Cajal body | IEA | cellular_component |
GO:0016070 | RNA metabolic process | TAS | biological_process |
GO:0022613 | Ribonucleoprotein complex biogenesis | IC | biological_process |
GO:0030532 | Small nuclear ribonucleoprotein complex | IC | cellular_component |
GO:0034660 | NcRNA metabolic process | TAS | biological_process |
GO:0036261 | 7-methylguanosine cap hypermethylation | IDA | biological_process |
GO:0044255 | Cellular lipid metabolic process | TAS | biological_process |
GO:0044281 | Small molecule metabolic process | TAS | biological_process |
GO:0071164 | RNA trimethylguanosine synthase activity | IDA | molecular_function |
GO:0071167 | Ribonucleoprotein complex import into nucleus | IC | biological_process |
Entries Per Page
Displaying Page of
4. Expression levels in datasets
- Meta-analysis result
p-value up | p-value down | FDR up | FDR down |
---|---|---|---|
0.6132960032 | 0.2322363284 | 0.9999902473 | 0.9281471008 |
- 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 | 0.1799447638 |
GSE13712_SHEAR | Up | 0.2277364736 |
GSE13712_STATIC | Down | -0.0092090204 |
GSE19018 | Down | -0.3918951459 |
GSE19899_A1 | Up | 0.1782321439 |
GSE19899_A2 | Up | 0.4119048414 |
PubMed_21979375_A1 | Down | -0.2959468522 |
PubMed_21979375_A2 | Down | -0.1068950724 |
GSE35957 | Down | -0.2093112976 |
GSE36640 | Down | -1.1699562888 |
GSE54402 | Up | 0.2143754062 |
GSE9593 | Down | -0.0333402575 |
GSE43922 | Up | 0.1495112236 |
GSE24585 | Down | -0.1331514817 |
GSE37065 | Up | 0.0653780274 |
GSE28863_A1 | Up | 0.0079479101 |
GSE28863_A2 | Up | 0.2599836041 |
GSE28863_A3 | Down | -0.7627992446 |
GSE28863_A4 | Down | -0.1873044776 |
GSE48662 | Down | -0.1031118276 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
- mirTarBase
MiRNA_name | mirBase ID | miRTarBase ID | Experiment | Support type | References (Pubmed ID) |
---|---|---|---|---|---|
hsa-miR-139-5p | MIMAT0000250 | MIRT047774 | CLASH | Functional MTI (Weak) | 23622248 |
Entries Per Page
Displaying Page of
- mirRecord
No target information from mirRecord
- mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 5 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
---|---|
24044898 | To minimize the damage, IsoAsp can be "repaired" by the protein l-isoaspartyl/d-aspartyl O-methyltransferase (PIMT) and S-adenosylmethionine (AdoMet) is the methyl donor of this reaction |
24044898 | PIMT is a repair enzyme that initiates the conversion of l-isoAsp (or d-Asp) residues to l-Asp residues |
18582478 | The protein l-isoaspartyl methyltransferase (PIMT) is involved in the repair of proteins containing abnormal L-isoaspartyl residues |
18582478 | Although its mechanism of action is well defined, little is known about the pathways involved in the regulation of PIMT expression |
18582478 | In this study, we demonstrated that glycogen synthase kinase-3 (GSK-3) and beta-catenin are involved in the regulation of PIMT expression |
18582478 | PIMT induction by lithium was dependent on increased protein synthesis |
18582478 | In addition, RT-PCR analysis showed higher level of PIMT mRNA following GSK-3 inhibition, which was abolished by the transcriptional inhibitor actinomycin D |
18582478 | These results demonstrated regulation of PIMT expression by lithium at both the transcriptional and the translational levels |
18582478 | Additionally, inhibition by siRNA of GSK-3 and beta-catenin modulated the expression of the PIMT in accordance with GSK-3 pharmacological inhibition |
18582478 | Valproic acid, an antiepileptic drug with mood-stabilizing properties, up-regulated phospho-GSK-3beta (Ser9), beta-catenin and PIMT levels similarly to lithium |
18582478 | This study reports that PIMT expression is up-regulated by GSK-3 inhibition and beta-catenin stabilization upon treatments with lithium and valproic acid |
18582478 | These findings suggest a possible therapeutic role for PIMT in certain brain diseases including epilepsy |
17892495 | Spontaneous protein deamidation of labile Asn residues, generating L-isoaspartates and D-aspartates, is associated with cell aging and is enhanced by an oxidative microenvironment; to minimize the damage, the isoaspartate residues can be 'repaired' by a specific L-isoaspartate (D-aspartate) protein O-methyltransferase (PIMT) |
17892495 | Using recombinant PIMT as a probe, we demonstrated a dramatic rise of L-isoaspartates in erythrocyte membrane proteins from DS patients |
17892495 | The integrity of the repair system was checked by evaluating methionine transport, PIMT specific activity, and intracellular concentrations of adenosylmethionine and adenosylhomocysteine |
17167531 | The enzyme L-isoaspartyl methyltransferase (PIMT) is known to repair damaged proteins that have accumulated abnormal aspartyl residues during cell aging |
17167531 | However, little is known about the mechanisms involved in the regulation of PIMT expression |
17167531 | Here we report that PIMT expression in bovine aortic endothelial cells is regulated by cell detachment and readhesion to a substratum |
17167531 | During cell detachment, the PIMT level was rapidly and strongly increased and correlated with a stimulation of protein synthesis |
17167531 | Aside from endothelial cells, PIMT levels were also regulated by cell adhesion in various cancer cell lines |
17167531 | The upregulation of PIMT expression could be prevented by an anti-alphavbeta3 antibody (LM609) or by a cyclic RGD peptide (XJ735) specific to integrin alphavbeta3, indicating that this integrin was likely involved in PIMT regulation |
17167531 | This study reports new insights on the molecular mechanisms responsible for the regulation of PIMT expression in cells |
17167531 | The regulation of PIMT level upon cell-substratum contact suggests a potential role for PIMT in biological processes such as wound healing, cell migration, and tumor metastasis dissemination |
12390520 | Protein L-isoaspartyl methyltransferase (PIMT) repairs the damaged proteins which have accumulated abnormal aspartyl residues during cell aging |
12390520 | Gene targeting has elucidated a physiological role for PIMT by showing that mice lacking PIMT died prematurely from fatal epileptic seizures |
12390520 | Here we investigated the role of PIMT in human mesial temporal lobe epilepsy |
12390520 | Using surgical specimens of hippocampus and neocortex from controls and epileptic patients, we showed that PIMT activity and expression were 50% lower in epileptic hippocampus than in controls but were unchanged in neocortex |
12390520 | Although the protein was down-regulated, PIMT mRNA expression was unchanged in epileptic hippocampus, suggesting post-translational regulation of the PIMT level |
12390520 | Microtubules component beta-tubulin, one of the major PIMT substrates, had an increased amount (two-fold) of L-isoaspartyl residues in the epileptic hippocampus |
12390520 | These results demonstrate that the down-regulation of PIMT in epileptic hippocampus leads to a significant accumulation of damaged tubulin that could contribute to neuron dysfunction in human mesial temporal lobe epilepsy |
Entries Per Page
Displaying Page of