HCSGD entry for S100A6
1. General information
Official gene symbol | S100A6 |
---|---|
Entrez ID | 6277 |
Gene full name | S100 calcium binding protein A6 |
Other gene symbols | 2A9 5B10 CABP CACY PRA |
Links to Entrez Gene | Links to Entrez Gene |
2. Neighbors in the network
![color bar](img/red_blue.jpg)
This gene isn't in Literature mining network.
3. Gene ontology annotation
GO ID | GO term | Evidence | Category |
---|---|---|---|
GO:0001726 | Ruffle | IDA | cellular_component |
GO:0005509 | Calcium ion binding | IDA IEA NAS | molecular_function |
GO:0005515 | Protein binding | IPI | molecular_function |
GO:0005523 | Tropomyosin binding | IDA | molecular_function |
GO:0005634 | Nucleus | IDA | cellular_component |
GO:0005635 | Nuclear envelope | IDA NAS | cellular_component |
GO:0005737 | Cytoplasm | IDA TAS | cellular_component |
GO:0005829 | Cytosol | IDA | cellular_component |
GO:0007165 | Signal transduction | TAS | biological_process |
GO:0007409 | Axonogenesis | NAS | biological_process |
GO:0008270 | Zinc ion binding | IEA | molecular_function |
GO:0015075 | Ion transmembrane transporter activity | IEA | molecular_function |
GO:0031234 | Extrinsic component of cytoplasmic side of plasma membrane | IDA | cellular_component |
GO:0042803 | Protein homodimerization activity | IDA IPI | molecular_function |
GO:0044548 | S100 protein binding | IPI | molecular_function |
GO:0048146 | Positive regulation of fibroblast proliferation | NAS | biological_process |
GO:0048306 | Calcium-dependent protein binding | IDA | molecular_function |
GO:0048471 | Perinuclear region of cytoplasm | IDA | cellular_component |
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4. Expression levels in datasets
- Meta-analysis result
p-value up | p-value down | FDR up | FDR down |
---|---|---|---|
0.7197160252 | 0.2155597280 | 0.9999902473 | 0.8951952666 |
- 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 | Down | -0.0428166616 |
GSE13712_SHEAR | Up | 0.3344070184 |
GSE13712_STATIC | Up | 0.0410818670 |
GSE19018 | Up | 0.0890217069 |
GSE19899_A1 | Down | -0.0728728844 |
GSE19899_A2 | Down | -0.4074590321 |
PubMed_21979375_A1 | Up | 0.3149376178 |
PubMed_21979375_A2 | Down | -0.1348640196 |
GSE35957 | Down | -0.2748942213 |
GSE36640 | Down | -0.1600279848 |
GSE54402 | Down | -0.2817803911 |
GSE9593 | Down | -0.1347104157 |
GSE43922 | Up | 0.0998915682 |
GSE24585 | Up | 0.0235101820 |
GSE37065 | Down | -0.0004065071 |
GSE28863_A1 | Down | -0.4047618801 |
GSE28863_A2 | Up | 0.2629517181 |
GSE28863_A3 | Up | 0.0746049172 |
GSE28863_A4 | Up | 0.2753965875 |
GSE48662 | Down | -0.3721182759 |
5. Regulation relationships with compounds/drugs/microRNAs
- Compounds
Not regulated by compounds
- Drugs
Not regulated by drugs
- MicroRNAs
- mirTarBase
No target information from mirTarBase
- mirRecord
No target information from mirRecord
6. Text-mining results about the gene
Gene occurances in abstracts of cellular senescence-associated articles: 3 abstracts the gene occurs.
PubMed ID of the article | Sentenece the gene occurs |
---|---|
26577046 | Herein, it is demonstrated, using progesterone receptor (PR) isoform-specific ovarian cancer model systems, that PR-A and PR-B promote distinct gene expression profiles that differ from PR-driven genes in breast cancer cells |
26577046 | In ovarian cancer models, PR-A primarily regulates genes independently of progestin, while PR-B is the dominant ligand-dependent isoform |
26577046 | In the presence of endogenous active FOXO1, PR-A was phosphorylated on Ser294 and transactivated PR-B at PR-B target genes; these events were blocked by the FOXO1 inhibitor (AS1842856) |
23095053 | The S100A6 calcium-binding protein regulates endothelial cell-cycle progression and senescence |
23095053 | We then examined the expression and functional properties of the major S100 family member, S100A6, in vascular endothelial cells |
23095053 | Comparison of primary and transformed human cells revealed significant differences in S100A6 protein levels in these cells |
23095053 | In primary human endothelial cells, S100A6 was present in both the nucleus and the cytoplasm |
23095053 | To assess the function of endothelial S100A6, we depleted protein levels using RNA interference and this caused increased cell-cycle arrest in the G2/M phase under different conditions |
23095053 | S100A6 depletion caused a decrease in both cyclin-dependent kinase 1 (CDK1) and phospho-CDK1 levels, which are essential for eukaryote cell-cycle progression |
23095053 | S100A6 depletion also decreased expression of CDK1, cyclin A1 (CCNA1) and cyclin B (CCNB1) genes with effects on cell-cycle progression |
23095053 | Depletion of endothelial S100A6 levels also elevated beta-galactosidase expression, which is an important hallmark of cellular senescence and exit from the mammalian cell cycle |
23095053 | We thus propose that S100A6 has an important role in regulating endothelial commitment to, and progression through, the cell cycle |
20013795 | S100A6 (calcyclin) deficiency induces senescence-like changes in cell cycle, morphology and functional characteristics of mouse NIH 3T3 fibroblasts |
20013795 | S100A6 (calcyclin) is a calcium binding protein with two EF-hand structures expressed mostly in fibroblasts and epithelial cells |
20013795 | We have established a NIH 3T3 fibroblast cell line stably transfected with siRNA against S100A6 to examine the effect of S100A6 deficiency on non-transformed cell physiology |
20013795 | We found that NIH 3T3 fibroblasts with decreased level of S100A6 manifested altered cell morphology and proliferated at a much slower pace than the control cells |
20013795 | Furthermore, fibroblasts with diminished S100A6 level exhibited morphological changes and biochemical features of cellular senescence as revealed by beta-galactosidase and gelatinase assays |
20013795 | Also, S100A6 deficiency induced changes in the actin cytoskeleton and had a profound impact on cell adhesion and migration |
20013795 | Thus, we have shown that the S100A6 protein is involved in multiple aspects of fibroblast physiology and that its presence ensures normal fibroblast proliferation and function |
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