HCSGD entry for POLA1


1. General information

Official gene symbolPOLA1
Entrez ID5422
Gene full namepolymerase (DNA directed), alpha 1, catalytic subunit
Other gene symbolsPOLA p180
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

color bar
This gene isn't in Literature mining network.

3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000082G1/S transition of mitotic cell cycleTASbiological_process
GO:0000083Regulation of transcription involved in G1/S transition of mitotic cell cycleTASbiological_process
GO:0000084Mitotic S phaseIDAbiological_process
GO:0000166Nucleotide bindingIDA IEAmolecular_function
GO:0000278Mitotic cell cycleTASbiological_process
GO:0000722Telomere maintenance via recombinationTASbiological_process
GO:0000723Telomere maintenanceTASbiological_process
GO:0000731DNA synthesis involved in DNA repairIMPbiological_process
GO:0000785ChromatinIDAcellular_component
GO:0001882Nucleoside bindingIEAmolecular_function
GO:0003677DNA bindingIDA IEA NASmolecular_function
GO:0003682Chromatin bindingIDAmolecular_function
GO:0003887DNA-directed DNA polymerase activityIDA IEA IMPmolecular_function
GO:0003896DNA primase activityIDAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005634NucleusIDAcellular_component
GO:0005635Nuclear envelopeIDAcellular_component
GO:0005654NucleoplasmIDA TAScellular_component
GO:0005658Alpha DNA polymerase:primase complexIDA TAScellular_component
GO:0005730NucleolusIDAcellular_component
GO:0005737CytoplasmIDAcellular_component
GO:0006260DNA replicationIMPbiological_process
GO:0006269DNA replication, synthesis of RNA primerIDAbiological_process
GO:0006270DNA replication initiationIDA TASbiological_process
GO:0006271DNA strand elongation involved in DNA replicationIMP TASbiological_process
GO:0006272Leading strand elongationIDAbiological_process
GO:0006273Lagging strand elongationIDAbiological_process
GO:0006281DNA repairIDAbiological_process
GO:0006297Nucleotide-excision repair, DNA gap fillingIBAbiological_process
GO:0006303Double-strand break repair via nonhomologous end joiningIMPbiological_process
GO:0008283Cell proliferationIDAbiological_process
GO:00084083'-5' exonuclease activityIBAmolecular_function
GO:0016032Viral processIEAbiological_process
GO:0016363Nuclear matrixIDAcellular_component
GO:0019985Translesion synthesisIBAbiological_process
GO:0032201Telomere maintenance via semi-conservative replicationTASbiological_process
GO:0032774RNA biosynthetic processIDAbiological_process
GO:0043231Intracellular membrane-bounded organelleIDAcellular_component
GO:0046872Metal ion bindingIEAmolecular_function
GO:0046982Protein heterodimerization activityIEAmolecular_function
GO:00515394 iron, 4 sulfur cluster bindingIEAmolecular_function
GO:0090305Nucleic acid phosphodiester bond hydrolysisIBAbiological_process
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.97224365720.00034200830.99999024730.0339560150

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

Data sourceUp or downLog fold change
GSE11954Down-0.1652143693
GSE13712_SHEARDown-0.4112997712
GSE13712_STATICDown-0.0972529026
GSE19018Down-0.2916023914
GSE19899_A1Down-0.3324440637
GSE19899_A2Down-4.5099394909
PubMed_21979375_A1Down-2.6870697685
PubMed_21979375_A2Down-3.1501682591
GSE35957Down-1.2185066148
GSE36640Down-3.6218671574
GSE54402Down-0.5268182520
GSE9593Down-1.1465865900
GSE43922Down-1.2287975277
GSE24585Down-0.3340057142
GSE37065Down-0.2334754046
GSE28863_A1Up0.3867545170
GSE28863_A2Up0.8035178865
GSE28863_A3Down-0.3220159374
GSE28863_A4Up0.1937569853
GSE48662Down-0.6733257519

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Compound

Target

Confidence score

Uniprot

CHEMBL1077295CHEMBL18289P09884
CHEMBL1092799CHEMBL18289P09884
CHEMBL29711CHEMBL18289P09884
CHEMBL498103CHEMBL18289P09884
CHEMBL1652467CHEMBL18289P09884
CHEMBL29711CHEMBL18289P09884
CHEMBL1095087CHEMBL18289P09884
CHEMBL29711CHEMBL18289P09884
CHEMBL193952CHEMBL18289P09884
CHEMBL437883CHEMBL18288P09884
CHEMBL1160303CHEMBL18288P09884
CHEMBL208804CHEMBL18288P09884
CHEMBL65374CHEMBL18288P09884
CHEMBL437310CHEMBL18288P09884
CHEMBL381375CHEMBL18288P09884
CHEMBL1160301CHEMBL18288P09884
CHEMBL1160301CHEMBL18288P09884
CHEMBL210842CHEMBL18288P09884
CHEMBL449712CHEMBL18288P09884
CHEMBL62784CHEMBL18288P09884
CHEMBL34912CHEMBL18288P09884
CHEMBL16119CHEMBL18288P09884
CHEMBL34912CHEMBL18288P09884
CHEMBL278248CHEMBL18288P09884
CHEMBL366792CHEMBL18288P09884
CHEMBL118808CHEMBL18288P09884
CHEMBL1160303CHEMBL18288P09884
CHEMBL333948CHEMBL18288P09884
CHEMBL16193CHEMBL18288P09884
CHEMBL16122CHEMBL18288P09884
CHEMBL380892CHEMBL18288P09884
CHEMBL380026CHEMBL18288P09884
CHEMBL119540CHEMBL18288P09884
CHEMBL607677CHEMBL18288P09884
CHEMBL29711CHEMBL18288P09884
CHEMBL332188CHEMBL18288P09884
CHEMBL440899CHEMBL18288P09884
CHEMBL16193CHEMBL18288P09884
CHEMBL1160213CHEMBL18288P09884
CHEMBL16103CHEMBL18288P09884
CHEMBL34912CHEMBL18288P09884
CHEMBL210047CHEMBL18288P09884
CHEMBL292775CHEMBL18288P09884
CHEMBL119855CHEMBL18288P09884
CHEMBL331536CHEMBL18288P09884
CHEMBL16129CHEMBL18288P09884
CHEMBL207651CHEMBL18288P09884
CHEMBL1160308CHEMBL18288P09884
CHEMBL15985CHEMBL18288P09884
CHEMBL210096CHEMBL18288P09884
CHEMBL119903CHEMBL18288P09884
CHEMBL377599CHEMBL18288P09884
CHEMBL425779CHEMBL18288P09884
CHEMBL379409CHEMBL18288P09884
CHEMBL193952CHEMBL18288P09884
CHEMBL29711CHEMBL18288P09884
CHEMBL278903CHEMBL18288P09884
CHEMBL65137CHEMBL18288P09884
CHEMBL1160308CHEMBL18288P09884
CHEMBL364611CHEMBL18287P09884
CHEMBL189667CHEMBL18287P09884
CHEMBL362353CHEMBL18287P09884
CHEMBL364611CHEMBL18287P09884
CHEMBL189667CHEMBL18287P09884
CHEMBL189667CHEMBL18287P09884
CHEMBL189703CHEMBL18287P09884
CHEMBL189703CHEMBL18287P09884
CHEMBL364611CHEMBL18287P09884
CHEMBL189703CHEMBL18287P09884
CHEMBL53912CHEMBL18284P09884
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  • Drugs

Name

Drug

Accession number

FludarabineDB01073 APRD00594
NelarabineDB01280 -

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-193b-3pMIMAT0002819MIRT016282MicroarrayFunctional MTI (Weak)20304954
hsa-miR-124-3pMIMAT0000422MIRT022295MicroarrayFunctional MTI (Weak)18668037
hsa-miR-26b-5pMIMAT0000083MIRT028969MicroarrayFunctional MTI (Weak)19088304
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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: 12 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

12067597Replicative enzymes and ageing: importance of DNA polymerase alpha function to the events of cellular ageing
12067597In eukaryotic cells, ranging from yeast to man, a replicative enzyme essential for initiation of transcription is DNA polymerase alpha (pol alpha), the activity of which is coordinately regulated with the initiation of DNA synthesis
11707897Activity of DNA polymerase alpha in aging human fibroblasts
10885806Aging and DNA polymerase alpha: modulation by dietary restriction
10515663DNA polymerase alpha and the 3'-->5' exonuclease involved in the proofreading of DNA synthesis were isolated from human diploid fetal lung fibroblast (TIG-1) cells at various population doubling levels (PDL)
10515663The fidelity of DNA polymerase alpha remained high until late passage and fell suddenly just before the end of the life span between 65 and 69 PDL
10515663In vitro DNA synthesis by DNA polymerase alpha from TIG-1 cells harvested at 69 PDL showed the amount of non-complementary nucleotides incorporated to be decreased by the addition of the 3'-->5' exonuclease from the same cells
10515663However, not all errors were edited out since the ratio of DNA polymerase activity to 3'-->5' exonuclease activity was adjusted to reflect that in vivo and the infidelity of DNA synthesis by error-prone DNA polymerase alpha from aged cells was improved by the addition of the highly active 3'-->5' exonuclease from cells at 41 PDL
10227381The activity of these extracts was compared after supplementation with three recombinant human replication factors: (1) the catalytic subunit of DNA polymerase alpha (DNA pol-alpha-cat), (2) the three subunits of replication protein A (RPA), and (3) DNA topoisomerase I (Topo I)
10227381Taken together, these results indicate that the low to undetectable activity of young HF extracts in this system is due mainly to reduced intracellular levels of RPA, while the senescent HF extracts are relatively deficient in DNA polymerase alpha and probably some other essential replication factors, as well as RPA
8106564Murine temperature-sensitive DNA polymerase alpha mutant displays a diminished capacity to stimulate DNA synthesis in senescent human fibroblast nuclei in heterokaryons at the nonpermissive condition
8106564We have investigated the capacity of a murine cell line with a temperature-sensitive (ts) mutation in the DNA polymerase alpha (Pola) locus and a series of ts non-Pola mutant cell lines from separate complementation groups to stimulate DNA synthesis, in senescent fibroblast nuclei in heterokaryons
1988288DNA polymerase alpha and the regulation of entry into S phase in heterokaryons
1988288In the studies described here, we have used cell fusion technology to investigate the formal kinetic relationship between the concentration of DNA polymerase alpha and the rate of reinitiation of DNA synthesis in nuclei from senescent cells
1988288Heterokaryons were derived from the fusion of senescent cells to a series of actively dividing cell types with inherently different DNA polymerase alpha activities per cell
1988288A kinetic analysis revealed a first-order relationship between the entry into S phase of senescent nuclei and the concentration of DNA polymerase alpha activity calculated to be in heterokaryons
2632279The relationship between cell size, the activity of DNA polymerase alpha and proliferative activity in human diploid fibroblast-like cell cultures
2632279In kinetic studies with human diploid fibroblast-like (HDFL) cells carried out in heterokaryons and in monokaryons, we have observed a first-order relationship between the level or concentration of DNA polymerase alpha and the rate of initiation of new rounds of DNA synthesis
2632279Because cell size is inversely proportional to the concentration of DNA polymerase alpha and presumably other replication factors, it is inversely related to the initiation of new rounds of DNA synthesis
3930524Induction of DNA polymerase alpha in senescent cultures of normal and Werner's syndrome cultured skin fibroblasts
3930524DNA polymerase alpha activity was determined following serum stimulation of early and late passages of human diploid fibroblast-like (HDFL) cultures derived from apparently normal donors (two strains) and from a patient with Werner's syndrome (one strain)
3930524The induction of DNA polymerase alpha in senescent cultures indicates that they retain the capacity to carry out some complex metabolic responses to mitogen stimulation
3930524In addition, these results suggest the possibility that dilution of DNA polymerase alpha and/or other DNA replication factors may play a role in the onset or maintenance of the postmitotic state in the enlarged senescent HDFL cells
7130287Evidence that a critical threshold of DNA polymerase-alpha activity may be required for the initiation of DNA synthesis in mammalian cell heterokaryons
7130287Our results indicate that the specific activity of DNA polymerase-alpha (or some other factor tightly coregulated with it) in "recessive" cell types (those unable to rescue senescent cells) is only about two times this theoretical "threshold" value, and that fusion of recessive cell types to senescent HDF cells reduces the specific activity in the heterokaryon to below this minimum, thus preventing the cells from entering S phase
7300456The first method produces DNA polymerase-alpha with a lower molecular weight and other properties that are not normally found for this enzyme
7300456It was concluded that this method produces proteolytically degraded DNA polymerase-alpha
7300456A second method was developed which produces DNA polymerase-alpha with all the normal properties of this enzyme
7300456DNA polymerase-alpha accounts for 95% of polymerase activity in young cells and its specific activity during the fibroblast lifespan correlates with the declining cellular growth rate
7300456The 5 S DNA polymerase-alpha has an increased in vitro error frequency (average 3
923389Apart from two exceptions found with lower organisms, the nuclear DNA polymerase activity was always higher under conditions which favoured the in vitro expression of DNA polymerase-beta rather than DNA polymerase-alpha
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