HCSGD entry for RBL1


1. General information

Official gene symbolRBL1
Entrez ID5933
Gene full nameretinoblastoma-like 1 (p107)
Other gene symbolsCP107 PRB1 p107
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000122Negative regulation of transcription from RNA polymerase II promoterIEAbiological_process
GO:0000278Mitotic cell cycleTASbiological_process
GO:0005515Protein bindingIPImolecular_function
GO:0005634NucleusIEAcellular_component
GO:0005654NucleoplasmTAScellular_component
GO:0005667Transcription factor complexIEAcellular_component
GO:0006351Transcription, DNA-templatedTASbiological_process
GO:0006357Regulation of transcription from RNA polymerase II promoterIEAbiological_process
GO:0006367Transcription initiation from RNA polymerase II promoterTASbiological_process
GO:0007049Cell cycleIEAbiological_process
GO:0007179Transforming growth factor beta receptor signaling pathwayTASbiological_process
GO:0008134Transcription factor bindingIPImolecular_function
GO:0010467Gene expressionTASbiological_process
GO:0016032Viral processIEAbiological_process
GO:0016568Chromatin modificationIEAbiological_process
GO:0043550Regulation of lipid kinase activityIDAbiological_process
GO:0045944Positive regulation of transcription from RNA polymerase II promoterTASbiological_process
GO:0051726Regulation of cell cycleIEAbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.84251268950.00536129330.99999024730.1483513116

  • Individual experiment result
    ( "-" represent NA in the specific microarray platform )

Data sourceUp or downLog fold change
GSE11954Down-0.1319581529
GSE13712_SHEARUp0.1871292597
GSE13712_STATICUp0.2888018768
GSE19018Down-0.2912746442
GSE19899_A1Up0.0194868653
GSE19899_A2Down-2.0036077531
PubMed_21979375_A1Down-1.0189717318
PubMed_21979375_A2Down-1.2591556146
GSE35957Down-0.8209616509
GSE36640Down-2.3206282927
GSE54402Down-0.6360154623
GSE9593Down-0.0268133775
GSE43922Down-1.5725266302
GSE24585Up0.1511669456
GSE37065Down-0.1713941244
GSE28863_A1Down-0.1166066270
GSE28863_A2Up0.8086319072
GSE28863_A3Down-0.3469104143
GSE28863_A4Up0.3741844276
GSE48662Down-0.3420151363

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-17-5pMIMAT0000070MIRT005851Luciferase reporter assayFunctional MTI21283765
hsa-miR-20a-5pMIMAT0000075MIRT005858Luciferase reporter assayFunctional MTI21283765
hsa-miR-106b-5pMIMAT0000680MIRT005866Luciferase reporter assayFunctional MTI21283765
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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: 14 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

23370776Of note, acute lowering of P107 did not induce relevant changes in the in vitro behavior of MSC
22333593RB family proteins pRb, p107 and p130 have similar structures and overlapping functions, enabling cell cycle arrest and cellular senescence
22333593In human fibroblasts acutely exposed to oncogenic ras, pRb has a specific role in suppressing DNA replication, and p107 or p130 cannot compensate for the loss of this function; however, a second p53/p21-dependent checkpoint prevents escape from growth arrest
22333593However, senescence induction by endogenous p16 was delayed in primary normal human mammary epithelial cells with reduced pRb but not with reduced p107 or p130
22333593Thus, under these circumstances, despite the presence of functional p53, p107 and p130 were unable to completely compensate for pRb in mediating senescence induction
20385362The RB protein family (RB, p107, and p130) has overlapping and compensatory functions in cell-cycle control
20385355RB, p107, and p130 are highly related proteins, each capable of regulating cellular proliferation
19737973Retinoblastoma family members (pRb, p107, and p130) previously implicated in gene silencing during fibroblasts senescence were found down-regulated in cells with nutlin-induced senescence-like phenotype, suggesting a mechanism for its reversibility
18418057Distinct roles for p107 and p130 in Rb-independent cellular senescence
18418057A small family of tumor suppressor genes encoding the retinoblastoma susceptibility protein family (Rb, p107, p130) exerts a partially redundant control of entry into S phase of DNA replication and cellular proliferation
18418057Consistent with this hypothesis, depletion of p107 potently inhibits the irradiation-induced senescence observed in DU145 cells
18418057The dominant effect of depleting both p107 and p130, in the absence of Rb, was a complete blockade of irradiation-induced cellular senescence
18418057These results indicate that p107 is required for initiation of accelerated cellular senescence in the absence of Rb and introduces the concept that p130 may be required to prevent the onset of terminal growth arrest in unstimulated prostate cancer cells lacking a functional Rb allele
18296649We observed that, in a manner reminiscent to senescent cells, permanent silencing of the E2F-dependent cdc6, dhfr, and p107 promoters in myotubes was associated with a specific increase in H3K9 trimethylation
17162659JC virus T'135, T'136 and T'165 proteins interact with cellular p107 and p130 in vivo and influence viral transformation potential
17162659These cell lines were used to evaluate the ability of each viral protein to bind p107 and p130 in vivo, and to influence cellular growth characteristics
17162659Differences were observed in the abilities of individual T' proteins to bind p107 and p130 and to alter their phosphorylation status
16465443Animals lacking Rb and/or its family members p107 and p130 have led scientists to uncover new and exciting roles for this protein family in development as well as tumor suppression
16123778Activation of p53(Val-135) induces a switch in pocket protein expression from pRb and p107 to p130(Rb2) and stalls the cells in late G1, early S-phase at high levels of cyclin E
12853964This difference is explained in part by functional compensation by the Rb-related gene p107
11756559Cdk4(R24C/R24C) mouse embryo fibroblasts (MEFs) displayed increased Cdk4 kinase activity resulting in hyperphosphorylation of all three members of the Rb family, pRb, p107, and p130
8853893The other two were novel E2F complexes that contained the cyclin-dependent kinase inhibitor p21 (cip1/WAF1/Sdi1/CAP20/PIC1) complexed with Rb/CDK2/cyclin E or with the Rb-related p107/CDK2/ cyclin D
8853893Addition of purified p21 protein to the S-phase-specific cyclin A/ CDK2-p107-E2F complex from young cells dissociated cyclin A and CDK2 from p107/E2F, suggesting an additional novel function for p21
8934878T[K1] is a T antigen point mutant that selectively is defective in binding pRb and the pRb-related proteins p107 and p130
8934878It did not appear that Id-1 interacted directly with pRb or p107
8934878Constitutive Id-1 expression failed to rescue proliferating cells from growth inhibition by pRb, p107, or p130, and failed to interact with pRb in the yeast two hybrid system
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