HCSGD entry for RSL1D1
1. General information
| Official gene symbol | RSL1D1 |
|---|---|
| Entrez ID | 26156 |
| Gene full name | ribosomal L1 domain containing 1 |
| Other gene symbols | CSIG PBK1 UTP30 |
| Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
|---|---|---|---|
| GO:0003723 | RNA binding | IEA | molecular_function |
| GO:0005730 | Nucleolus | IDA IEA | cellular_component |
| GO:0032880 | Regulation of protein localization | 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 |
|---|---|---|---|
| 0.0037397059 | 0.9572015311 | 0.1640915282 | 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 | 1.2425652763 |
| GSE13712_SHEAR | Up | 0.3656884645 |
| GSE13712_STATIC | Up | 0.1804398617 |
| GSE19018 | Down | -0.5503440971 |
| GSE19899_A1 | Up | 0.8228874531 |
| GSE19899_A2 | Up | 1.3559514904 |
| PubMed_21979375_A1 | Up | 1.1479374801 |
| PubMed_21979375_A2 | Up | 1.2539469890 |
| GSE35957 | Down | -0.2088658096 |
| GSE36640 | Up | 0.5997669075 |
| GSE54402 | Up | 0.3106341975 |
| GSE9593 | Up | 0.6216674610 |
| GSE43922 | Up | 0.4148169980 |
| GSE24585 | Down | -0.4773924031 |
| GSE37065 | Down | -0.0798007715 |
| GSE28863_A1 | Up | 0.1984926779 |
| GSE28863_A2 | Up | 0.0871156320 |
| GSE28863_A3 | Down | -0.2763552755 |
| GSE28863_A4 | Up | 0.2517620388 |
| GSE48662 | Up | 0.2719734779 |
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-103a-3p | MIMAT0000101 | MIRT027166 | Sequencing | Functional MTI (Weak) | 20371350 |
| hsa-miR-193b-3p | MIMAT0002819 | MIRT041332 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-miR-16-5p | MIMAT0000069 | MIRT051068 | CLASH | Functional MTI (Weak) | 23622248 |
| hsa-let-7e-5p | MIMAT0000066 | MIRT051659 | 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: 5 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
|---|---|
| 26686419 | Ribosomal L1 domain and lysine-rich region are essential for CSIG/ RSL1D1 to regulate proliferation and senescence |
| 26686419 | Using a suppressive subtractive hybridization system, we identified CSIG (cellular senescence-inhibited gene protein; RSL1D1) as a novel senescence-associated gene |
| 26686419 | CSIG is implicated in various process including cell cycle regulation, apoptosis, and tumor metastasis |
| 26686419 | We previously showed that CSIG plays an important role in regulating cell proliferation and cellular senescence progression through inhibiting PTEN, however, which domain or region of CSIG contributes to this function |
| 26686419 | To clarify this question, we investigated the functional importance of ribosomal L1 domain and lysine (Lys) -rich region of CSIG |
| 26686419 | The data showed that expression of CSIG potently reduced PTEN expression, increased cell proliferation rates, and reduced the senescent phenotype (lower SA-beta-gal activity) |
| 26686419 | By contrast, neither the expression of CSIG N- terminal (NT) fragment containing the ribosomal L1 domain nor C-terminal (CT) fragment containing Lys-rich region could significantly altered the levels of PTEN; instead of promoting cell proliferation and delaying cellular senescence, expression of CSIG-NT or CSIG-CT inhibited cell proliferation and accelerated cell senescence (increased SA-beta-gal activity) compared to either CSIG over-expressing or control (empty vector transfected) cells |
| 26686419 | The further immunofluorescence analysis showed that CSIG-CT and CSIG-NT truncated proteins exhibited different subcellular distribution with that of wild-type CSIG |
| 26686419 | Conclusively, both ribosomal L1 domain and Lys-rich region of CSIG are critical for CSIG to act as a regulator of cell proliferation and cellular senescence |
| 26029164 | Cellular senescence-inhibited gene (CSIG), also named as ribosomal_L1 domain-containing 1 (RSL1D1), is implicated in various processes including cell cycle regulation, cellular senescence, apoptosis, and tumor metastasis |
| 26029164 | To screen important targets and signaling pathways modulated by CSIG, we compared the gene expression profiles in CSIG-silencing and control HEK293 cells using Affymetrix microarray Human Genome U133 Plus 2 |
| 26029164 | The mechanism study showed that CSIG modulated the mRNA half-life of Cdc14B, CASP7, and CREBL2 |
| 26029164 | This study shows that expression profiling can be used to identify genes that are transcriptionally or post-transcriptionally modified following CSIG knockdown and to reveal the molecular mechanism of cell proliferation and senescence regulated by CSIG |
| 25749381 | Cellular senescence-inhibited gene (CSIG) protein significantly prolongs the progression of replicative senescence, but its role in tumorigenesis is unclear |
| 25749381 | CSIG protein was overexpressed in 86 |
| 25749381 | Furthermore, upregulation of CSIG significantly increased the colony formation of SMMC7721 and HepG2 cells, and silencing CSIG could induce cell cycle arrest and cell apoptosis |
| 25749381 | The tumorigenic ability of CSIG was confirmed in vivo in a mouse xenograft model |
| 25749381 | Our results showed that CSIG promoted the proliferation of HepG2 and SMMC7721 cells in vivo |
| 25749381 | Finally, CSIG protein directly interacted with c-MYC protein and increased c-MYC protein levels; the ubiquitination and degradation of c-MYC protein was increased with knockdown of CSIG |
| 25749381 | CSIG could also increase the expression of c-MYC protein in SMMC7721 cells in vivo, and it was noted that the level of c-MYC protein was also elevated in most human cancerous tissues with high level of CSIG |
| 22419112 | Nucleolar protein CSIG is required for p33ING1 function in UV-induced apoptosis |
| 22419112 | Cellular senescence-inhibited gene (CSIG) protein, a nucleolar protein with a ribosomal L1 domain in its N-terminus, can exert non-ribosomal functions to regulate biological processes, such as cellular senescence |
| 22419112 | Here, we describe a previously unknown function for CSIG: promotion of apoptosis in response to ultraviolet (UV) irradiation-induced CSIG upregulation |
| 22419112 | We identified p33ING1 as a binding partner that interacts with CSIG |
| 22419112 | After UV irradiation, p33ING1 increases its protein expression, translocates into the nucleolus and binds CSIG |
| 18678645 | CSIG inhibits PTEN translation in replicative senescence |
| 18678645 | Using a suppressive subtractive hybridization system, we identified CSIG (cellular senescence-inhibited gene protein; RSL1D1) that was abundant in young human diploid fibroblast cells but declined upon replicative senescence |
| 18678645 | Overexpression or knockdown of CSIG did not influence p21(Cip1) and p16(INK4a) expressions |
| 18678645 | Instead, CSIG negatively regulated PTEN and p27(Kip1) expressions, in turn promoting cell proliferation |
| 18678645 | In PTEN-silenced HEK 293 cells and PTEN-deficient human glioblastoma U87MG cells, the effect of CSIG on p27(Kip1) expression and cell division was abolished, suggesting that PTEN was required for the role of CSIG on p27(Kip1) regulation and cell cycle progression |
| 18678645 | Investigation into the underlying mechanism revealed that the regulation of PTEN by CSIG was achieved through a translational suppression mechanism |
| 18678645 | Moreover, overexpression of CSIG significantly delayed the progression of replicative senescence, while knockdown of CSIG expression accelerated replicative senescence |
| 18678645 | Our findings indicate that CSIG acts as a novel regulatory component of replicative senescence, which requires PTEN as a mediator and involves in a translational regulatory mechanism |
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