HCSGD entry for TERF1
1. General information
| Official gene symbol | TERF1 |
|---|---|
| Entrez ID | 7013 |
| Gene full name | telomeric repeat binding factor (NIMA-interacting) 1 |
| Other gene symbols | PIN2 TRBF1 TRF TRF1 hTRF1-AS t-TRF1 |
| 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:0000086 | G2/M transition of mitotic cell cycle | IEP | biological_process |
| GO:0000723 | Telomere maintenance | TAS | biological_process |
| GO:0000781 | Chromosome, telomeric region | IDA | cellular_component |
| GO:0000783 | Nuclear telomere cap complex | IDA ISS | cellular_component |
| GO:0001309 | Age-dependent telomere shortening | IDA | biological_process |
| GO:0003677 | DNA binding | NAS | molecular_function |
| GO:0003682 | Chromatin binding | IEA | molecular_function |
| GO:0003691 | Double-stranded telomeric DNA binding | IDA | molecular_function |
| GO:0005515 | Protein binding | IPI | molecular_function |
| GO:0005634 | Nucleus | IDA NAS | cellular_component |
| GO:0005654 | Nucleoplasm | TAS | cellular_component |
| GO:0005737 | Cytoplasm | IEA | cellular_component |
| GO:0005819 | Spindle | IDA IEA | cellular_component |
| GO:0006919 | Activation of cysteine-type endopeptidase activity involved in apoptotic process | IDA | biological_process |
| GO:0007004 | Telomere maintenance via telomerase | IMP NAS | biological_process |
| GO:0007067 | Mitosis | IEA | biological_process |
| GO:0007094 | Mitotic spindle assembly checkpoint | IMP | biological_process |
| GO:0008017 | Microtubule binding | IDA | molecular_function |
| GO:0008156 | Negative regulation of DNA replication | IDA | biological_process |
| GO:0008301 | DNA binding, bending | IDA | molecular_function |
| GO:0008656 | Cysteine-type endopeptidase activator activity involved in apoptotic process | IDA | molecular_function |
| GO:0010834 | Telomere maintenance via telomere shortening | IMP | biological_process |
| GO:0031116 | Positive regulation of microtubule polymerization | IDA | biological_process |
| GO:0032211 | Negative regulation of telomere maintenance via telomerase | IGI | biological_process |
| GO:0032214 | Negative regulation of telomere maintenance via semi-conservative replication | NAS | biological_process |
| GO:0042162 | Telomeric DNA binding | IDA IEA | molecular_function |
| GO:0042493 | Response to drug | IEA | biological_process |
| GO:0042803 | Protein homodimerization activity | IEA IPI | molecular_function |
| GO:0043065 | Positive regulation of apoptotic process | IDA | biological_process |
| GO:0045840 | Positive regulation of mitosis | IMP | biological_process |
| GO:0045931 | Positive regulation of mitotic cell cycle | IMP | biological_process |
| GO:0046982 | Protein heterodimerization activity | IDA | molecular_function |
| GO:0051260 | Protein homooligomerization | IDA | biological_process |
| GO:0051974 | Negative regulation of telomerase activity | IGI | biological_process |
| GO:1900119 | Positive regulation of execution phase of apoptosis | 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 |
|---|---|---|---|
| 0.8649416588 | 0.2233046503 | 0.9999902473 | 0.9091417943 |
- 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 | 0.1250401581 |
| GSE13712_SHEAR | Up | 0.0681192820 |
| GSE13712_STATIC | Down | -0.1329048574 |
| GSE19018 | Down | -0.3301474495 |
| GSE19899_A1 | Down | -0.7681758842 |
| GSE19899_A2 | Up | 0.0260603098 |
| PubMed_21979375_A1 | Down | -0.1917238146 |
| PubMed_21979375_A2 | Up | 0.3083218652 |
| GSE35957 | Down | -0.1855767533 |
| GSE36640 | Up | 0.0400322306 |
| GSE54402 | Down | -0.2220970637 |
| GSE9593 | Up | 0.0012895712 |
| GSE43922 | Down | -0.6040344738 |
| GSE24585 | Down | -0.0659265155 |
| GSE37065 | Up | 0.1415287213 |
| GSE28863_A1 | Down | -0.0024186257 |
| GSE28863_A2 | Down | -0.0365841826 |
| GSE28863_A3 | Up | 0.1438834560 |
| GSE28863_A4 | Up | 0.0610455093 |
| GSE48662 | Up | 0.1125187091 |
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-346 | MIMAT0000773 | MIRT004234 | Microarray | Functional MTI (Weak) | 16822819 |
| hsa-let-7e-5p | MIMAT0000066 | MIRT051641 | CLASH | Functional MTI (Weak) | 23622248 |
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- mirRecord
No target information from mirRecord
- mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 18 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 26462146 | Ber8 could then induce the delocalization of TRF1 and POT1 from the telomere accompanied by a rapid telomere uncapping |
| 26345860 | The results showed that transcription of human telomere binding protein 1 did not change with cell senescence, whereas the protein expression of human telomere binding protein 1 increased gradually and then decreased rapidly; there was no change in the mRNA and protein expression of POT1; with the replicative senescence of human embryonic lung fibroblasts, expression of POT1 decreased gradually; TRF1 showed an increasing trend with cell senescence; and p53 protein expression did not change |
| 26345860 | Together, the results from this study suggest that human telomere binding protein 1, POT1, and TRF1 played important roles in cell senescence |
| 26082495 | By fusing the KillerRed chromophore with the telomere repeat binding factor 1, TRF1, we developed a novel approach to generate localized damage to telomere DNA and to monitor the real time damage response at the single telomere level |
| 24839934 | Evidence suggests that Pin2/TRF1-interacting protein X1 (PinX1) inhibits telomerase activity in many types of cancer cells |
| 23702294 | A comprehensive model for the recognition of human telomeres by TRF1 |
| 23702294 | TRF1 is a homodimer with roles governing DNA architecture and negatively regulating telomere length |
| 23268632 | Telomeric Repeat Factor 1 (TRF1) is a protein that binds at telomere ends |
| 23268632 | PURPOSE: to measure the concentrations of TRF1 and the relationships among telomere length, telomerase activity, and TRF1 levels in tumor and normal colorectal mucosa |
| 23268632 | METHOD: from normal and tumoral samples of 83 patients who underwent surgery for colorectal cancer we analyzed TRF1 protein concentration by Western Blot, telomerase activity, by the fluorescent-telomeric repeat amplification protocol assay and telomere length by Southern Blot |
| 23268632 | RESULTS: high levels of TRF1 were observed in 68 |
| 23268632 | 7% of tumor samples, while the majority of normal samples (59%) showed negative or weak TRF1 concentrations |
| 23268632 | Among the tumor samples, telomere length was significantly associated with TRF1 protein levels (p = 0 |
| 23268632 | CONCLUSIONS: a relationship was found between telomere length and TRF1 abundance protein in tumor samples, which means that TRF1 is an important factor in the tumor progression and maybe a diagnostic factor |
| 22985061 | CONCLUSIONS: The increase in telomerase activity and TRF1 protein expression of vascular endothelial cell might show an aspect of cellular protective reaction against oxygen stress |
| 22932806 | Conditional TRF1 knockout in the hematopoietic compartment leads to bone marrow failure and recapitulates clinical features of dyskeratosis congenita |
| 22932806 | TRF1 is part of the shelterin complex, which binds telomeres and it is essential for their protection |
| 22932806 | Ablation of TRF1 induces sister telomere fusions and aberrant numbers of telomeric signals associated with telomere fragility |
| 22932806 | Allelic variations in TRF1 have been found associated with BMF |
| 22932806 | To address a possible role for TRF1 dysfunction in BMF, here we generated a mouse model with conditional TRF1 deletion in the hematopoietic system |
| 22932806 | Chronic TRF1 deletion results in increased DNA damage and cellular senescence, but not increased apoptosis, in BM progenitor cells, leading to severe aplasia |
| 22932806 | Together, these results represent proof of principle that mutations in TRF1 lead to the main clinical features of BMF |
| 17202845 | All the other DSB repair proteins tested, Sir2, TRF1 and Ku80, did not show any significant differences upon aging |
| 17000763 | Nucleostemin delays cellular senescence and negatively regulates TRF1 protein stability |
| 17000763 | We demonstrated that NS could interact with telomeric repeat-binding factor 1 (TRF1) and enhance the degradation but not the ubiquitination of the TRF1 protein, which negatively regulates telomere length and is essential for early embryogenesis |
| 17000763 | This work demonstrates the roles of NS in establishing early embryogenesis and delaying cellular senescence of MEFs and reveals a mechanism of a NS-regulated degradation of TRF1 |
| 16507984 | TRF1 is a telomere-associated protein that inhibits telomere elongation by its binding to telomere repeats, preventing access to telomerase |
| 16507984 | Human TRF1 interacts with tankyrase 1 and tankyrase 2 proteins, two related members of the tankyrase family shown to have poly(ADP-ribose) polymerase activity |
| 16507984 | Human tankyrase 1 is reported to ADP-ribosylate TRF1 and to down-regulate the telomeric repeat binding activity of TRF1, resulting in telomerase-dependent telomere elongation |
| 15000677 | Increase in TERF1 concentration prevents telomere elongation by telomerase |
| 15000677 | Natural regulation of TERF1 involves tankyrase, ATM protein kinase, and fluctuations of the protein level across a cell cycle |
| 14681297 | Limited capacity of the nuclear matrix to bind telomere repeat binding factor TRF1 may restrict the proliferation of mortal human fibroblasts |
| 14681297 | In this study, we investigated the role of telomere repeat binding factor (TRF1) in the proliferation of human fibroblasts |
| 14681297 | TRF1 expression is upregulated in a large variety of immortal human cells and supports de novo telomere formation in a dose-dependent manner |
| 14681297 | These observations suggest that the suppression of TRF1 might limit telomere maintenance and thus the life span of mortal cells |
| 14681297 | However, primary fibroblasts ectopically overexpressing TRF1 were unable to avoid senescence |
| 14681297 | On the other hand, exogenously expressed TRF1 in primary fibroblasts neither supported de novo telomere formation nor bound to the nuclear matrix as tightly as observed in immortal cells that show upregulated TRF1 expression |
| 14681297 | We present evidence suggesting that mortal human cells lack specific ligand(s) that anchor TRF1 to the nuclear matrix and that this contributes to their limited lifespan |
| 11531263 | Among binding factor proteins, TRF1 mRNA showed reciprocal changes possibly directed toward maintaining a stable telomere length |
| 11531263 | In this study, our results demonstrate that not only hTERT but also TRF1 are important regulator of telomerase activity |
| 11481865 | Our results suggest that not only hTERT but also TRF1 and 2 are important regulators of telomerase activity |
| 11179492 | TRF1 expression, which is believed to control telomere length, was significantly elevated in patients with acute lymphoblastic leukemia (ALL) (P=0 |
| 11179492 | This indicates that TRF1 may act to monitor telomere length under the condition of up-regulated telomerase activity in some neoplastic cells |
| 11179492 | Although the precise regulation mechanism of telomere length is still uncertain, these results may suggest that regulation of telomere length is partially associated with TRF1 expression, whereas dysfunction of TRF1 expression may be speculated in a subset of acute leukemia |
| 11063723 | TRF1 is a critical trans-acting factor required for de novo telomere formation in human cells |
| 11063723 | In this study, we investigated the cellular factor(s) required for telomere formation using the frequency of telomere seeding as an index and identified TRF1, one of the telomere repeat binding proteins, as an essential trans-acting factor |
| 11063723 | The exogenous telomere repeat induces telomere formation at a frequency determined by the availability of TRF1, even in telomerase-negative cells |
| 11063723 | Our study shows clearly that TRF1 has a novel physiological significance distinct from its role as a regulator of telomere length in the endogenous chromosome |
| 9781837 | The molecular weight of the major binding factor in the normal human fibroblasts was approximately 32 kDa which is different from that of the telomere-associated protein, TRF-1 |
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