HCSGD entry for SRF


1. General information

Official gene symbolSRF
Entrez ID6722
Gene full nameserum response factor (c-fos serum response element-binding transcription factor)
Other gene symbolsMCM1
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

color bar

3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0000790Nuclear chromatinIEAcellular_component
GO:0000978RNA polymerase II core promoter proximal region sequence-specific DNA bindingIEA ISSmolecular_function
GO:0000983RNA polymerase II core promoter sequence-specific DNA binding transcription factor activityIMPmolecular_function
GO:0001076RNA polymerase II transcription factor binding transcription factor activityIEAmolecular_function
GO:0001077RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcriptionIDA IEAmolecular_function
GO:0001228RNA polymerase II transcription regulatory region sequence-specific DNA binding transcription factor activity involved in positive regulation of transcriptionISSmolecular_function
GO:0001569Patterning of blood vesselsIEAbiological_process
GO:0001666Response to hypoxiaIEPbiological_process
GO:0001701In utero embryonic developmentIEAbiological_process
GO:0001707Mesoderm formationIEAbiological_process
GO:0001764Neuron migrationIEAbiological_process
GO:0001829Trophectodermal cell differentiationIDAbiological_process
GO:0001947Heart loopingIEA ISSbiological_process
GO:0002011Morphogenesis of an epithelial sheetIEAbiological_process
GO:0002042Cell migration involved in sprouting angiogenesisIEA IMPbiological_process
GO:0003257Positive regulation of transcription from RNA polymerase II promoter involved in myocardial precursor cell differentiationIEA IGIbiological_process
GO:0003700Sequence-specific DNA binding transcription factor activityIDAmolecular_function
GO:0003705RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activityIEAmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005634NucleusIDAcellular_component
GO:0005737CytoplasmIEA TAScellular_component
GO:0006366Transcription from RNA polymerase II promoterIDAbiological_process
GO:0007160Cell-matrix adhesionIEAbiological_process
GO:0007507Heart developmentISSbiological_process
GO:0007616Long-term memoryIEAbiological_process
GO:0008134Transcription factor bindingIPImolecular_function
GO:0008285Negative regulation of cell proliferationIEAbiological_process
GO:0008306Associative learningIEAbiological_process
GO:0009636Response to toxic substanceTASbiological_process
GO:0009725Response to hormoneIDAbiological_process
GO:0010669Epithelial structure maintenanceIEAbiological_process
GO:0010735Positive regulation of transcription via serum response element bindingIDAbiological_process
GO:0010736Serum response element bindingIDA IEAmolecular_function
GO:0021766Hippocampus developmentIEAbiological_process
GO:0022028Tangential migration from the subventricular zone to the olfactory bulbIEAbiological_process
GO:0030038Contractile actin filament bundle assemblyIEAbiological_process
GO:0030155Regulation of cell adhesionIEAbiological_process
GO:0030168Platelet activationIEAbiological_process
GO:0030220Platelet formationIEAbiological_process
GO:0030336Negative regulation of cell migrationIEAbiological_process
GO:0031175Neuron projection developmentIEAbiological_process
GO:0031490Chromatin DNA bindingIEAmolecular_function
GO:0033561Regulation of water loss via skinIEAbiological_process
GO:0034097Response to cytokineIMP NASbiological_process
GO:0035855Megakaryocyte developmentIEAbiological_process
GO:0035912Dorsal aorta morphogenesisIEAbiological_process
GO:0042789MRNA transcription from RNA polymerase II promoterIEA ISSbiological_process
GO:0042803Protein homodimerization activityIPImolecular_function
GO:0043149Stress fiber assemblyIEAbiological_process
GO:0043589Skin morphogenesisIEAbiological_process
GO:0045059Positive thymic T cell selectionIEAbiological_process
GO:0045214Sarcomere organizationIEAbiological_process
GO:0045597Positive regulation of cell differentiationIDAbiological_process
GO:0045944Positive regulation of transcription from RNA polymerase II promoterIDAbiological_process
GO:0045987Positive regulation of smooth muscle contractionIDAbiological_process
GO:0046016Positive regulation of transcription by glucoseIEAbiological_process
GO:0046716Muscle cell cellular homeostasisIEA ISSbiological_process
GO:0048589Developmental growthIEAbiological_process
GO:0048666Neuron developmentTASbiological_process
GO:0048821Erythrocyte developmentIEAbiological_process
GO:0051091Positive regulation of sequence-specific DNA binding transcription factor activityIDAbiological_process
GO:0051150Regulation of smooth muscle cell differentiationTASbiological_process
GO:0051491Positive regulation of filopodium assemblyIEAbiological_process
GO:0055003Cardiac myofibril assemblyIEAbiological_process
GO:0060055Angiogenesis involved in wound healingTASbiological_process
GO:0060218Hematopoietic stem cell differentiationIEAbiological_process
GO:0060261Positive regulation of transcription initiation from RNA polymerase II promoterIDAbiological_process
GO:0060292Long term synaptic depressionIEAbiological_process
GO:0060347Heart trabecula formationIEAbiological_process
GO:0060947Cardiac vascular smooth muscle cell differentiationIEAbiological_process
GO:0061029Eyelid development in camera-type eyeIEAbiological_process
GO:0070830Tight junction assemblyIEAbiological_process
GO:0071333Cellular response to glucose stimulusIEAbiological_process
GO:0090009Primitive streak formationIEAbiological_process
GO:0090136Epithelial cell-cell adhesionIEAbiological_process
GO:0090398Cellular senescenceIMPbiological_process
GO:1900222Negative regulation of beta-amyloid clearanceIMPbiological_process
Entries Per Page
Displaying Page of

4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.93693043960.02643890810.99999024730.3115033572

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

Data sourceUp or downLog fold change
GSE11954Down-0.7398194475
GSE13712_SHEARDown-0.0016098630
GSE13712_STATICDown-0.1314120727
GSE19018Down-0.7414630595
GSE19899_A1Down-0.2605198497
GSE19899_A2Down-0.0911908289
PubMed_21979375_A1Down-0.2595787547
PubMed_21979375_A2Up0.0591350008
GSE35957Up0.3143434686
GSE36640Down-0.2868436367
GSE54402Up0.1293133816
GSE9593Down-0.1652813796
GSE43922Up0.0381025633
GSE24585Down-0.6458941173
GSE37065Down-0.1897235460
GSE28863_A1Down-0.0156834304
GSE28863_A2Down-0.1428923871
GSE28863_A3Up0.4879642637
GSE28863_A4Down-0.2570515151
GSE48662Down-0.2197027803

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-122-5pMIMAT0000421MIRT000365Luciferase reporter assay//qRT-PCR//Western blotFunctional MTI19726678
hsa-miR-1MIMAT0000416MIRT023547Western blotNon-Functional MTI20458751
hsa-miR-26b-5pMIMAT0000083MIRT028897MicroarrayFunctional MTI (Weak)19088304
hsa-miR-18a-3pMIMAT0002891MIRT040918CLASHFunctional MTI (Weak)23622248
hsa-miR-484MIMAT0002174MIRT041943CLASHFunctional MTI (Weak)23622248
hsa-miR-324-3pMIMAT0000762MIRT042926CLASHFunctional MTI (Weak)23622248
hsa-miR-331-3pMIMAT0000760MIRT043424CLASHFunctional MTI (Weak)23622248
hsa-miR-320aMIMAT0000510MIRT044832CLASHFunctional MTI (Weak)23622248
hsa-miR-92a-3pMIMAT0000092MIRT049829CLASHFunctional MTI (Weak)23622248
Entries Per Page
Displaying Page of
    • 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

25183317BACKGROUND: The protein p49/STRAP (SRFBP1) is a transcription cofactor of serum response factor (SRF) which regulates cytoskeletal and muscle-specific genes
25183317CONCLUSIONS: Since p49/STRAP is a co-factor of SRF, our data suggest that p49/STRAP likely regulates cell size and morphology through SRF target genes
22467316Serum response factor and miRNA expression represent main mechanisms controlling the pattern of gene expression
21160097There are also MCM1 and MCM10, which are important in DNA replication, but they do not possess the specific MCM box
16786104We observed the changes of these three kinds of HUVECs (HUVECs, N17Rac1-HUVECs, V12Rac1-HUVECs) after hypoxia for 48 h and 96 h, the expression and localization of serum response factor (SRF), which is one of the downstream signal molecules of Rac1, were also investigated
16786104To further investigate the mechanism of HUVEC senescence induced by Rac1, we detected the expression of total SRF (tSRF) and nuclear SRF (nSRF) in these three kinds of HUVECs by immunofluorescent analysis and Western blot assay after hypoxia
16786104The results showed that the expression of nSRF decreased obviously and the nuclear translocation of SRF was inhibited in HUVECs infected by V12Rac1 compared with those in the normal HUVECs
16786104These results suggest that activation of Rac1 accelerates endothelial cell senescence and inhibition of Rac1 activity prevents HUVECs from entering senescence induced by hypoxia, while the nuclear translocation of SRF regulated by Rac1 might play an important role in the process of senescence
15282327Protein kinase C delta blocks immediate-early gene expression in senescent cells by inactivating serum response factor
15282327The serum response factor (SRF), a major transcriptional activator of immediate-early gene promoters, loses the ability to bind to the serum response element (SRE) and becomes hyperphosphorylated in senescent cells
15282327We identify protein kinase C delta (PKC delta) as the kinase responsible for inactivation of SRF both in vitro and endogenously in senescent cells
15282327The phosphorylation of T160 of SRF by PKC delta in vitro and in vivo led to loss of SRF DNA binding activity
12470826Transcription of c-fos in response to mitogens depends on the activation of a multiprotein complex formed on the c-fos serum response element (SRE), which includes the transcription factors serum response factor (SRF) and ternary complex factor (TCF)
11570821Transcription of c-fos in response to mitogens depends on the activation of a multiprotein complex formed on the c-fos serum response element (SRE), which includes the transcription factors SRF (serum response factor) and TCF (ternary complex factor)
11570821These impairments, together with the impaired DNA binding activity of SRF, could potentially account for the lack of c-fos expression in senescent cells and for multiple other molecular changes dependent upon this pathway
11181183Senescence represses the nuclear localization of the serum response factor and differentiation regulates its nuclear localization with lineage specificity
11181183The differentiation of cultured 3T3T mesenchymal stem cells into adipocytes represses growth factor responsiveness by limiting the nuclear localization of the serum response factor (SRF) that binds to and activates the promoters of growth control genes that contain the serum response elements (SRE), such as junB and c-fos
11181183The regulation of SRF nuclear localization by adipocyte differentiation is specific, because we show that adipocyte differentiation does not repress the nuclear localization of six other transacting factors
11181183To determine if repression of growth factor responsiveness that occurs during senescence also represses the nuclear localization of SRF, we studied normal human WI-38 fibroblasts at low versus high population doublings
11181183The results show that SRF localizes to the nucleus of proliferative cells whereas in senescent cells SRF can not be detected in the nucleus
11181183We next evaluated the cellular distribution of SRF in selected human tissues to determine whether the loss of proliferative potential in vivo could have a different effect on SRF nuclear localization
11181183We found that in cells of the small bowel mucosa, differentiation modulates SRF nuclear localization in an opposite manner
11181183Minimal SRF expression and nuclear localization is evident in undifferentiated cells at the base of crypts whereas increased SRF expression and nuclear localization is evident in differentiated cells at the surface tip of the villus
11181183These results together establish that regulation of SRF expression and nuclear localization is important in senescence and differentiation in a lineage specific manner
10082129Electrophoretic mobility shift studies using young and old cell nuclear extracts showed a marked decrease in serum response factor (SRF) binding activity to the SRE in old compared to young cells
10082129Loss of SRF binding activity has been correlated with the loss of expression of another growth-related immediate-early gene (c-fos)
8864058Here we survey the relevant literature regarding altered gene expression and the role of transcription factors during cellular aging, focusing upon the serum response factor (SRF)
8864058SRF is hyperphosphorylated in senescent HDFs and fails to bind to the serum-response element in the c-fos promoter
8864058Differential phosphorylation during replicative aging may contribute, at least in part, to the altered activity of SRF and possibly other transcription factors and to subsequent changes in the expression of serum-regulated genes in senescent HDFs
8960358We focus on regulation of the c-fos gene through posttranslational modification of the serum response factor (SRF) as an example of altered gene expression during cellular aging
8007992While no major differences in the expression of the serum response factor (SRF) that binds the serum response element were seen between early-passage and late-passage cells, hyperphosphorylation of SRF was observed in near-senescent cells
8007992Furthermore, removal of phosphatase inhibitors during the isolation of endogenous nuclear proteins restored the ability of SRF isolated from old cells to bind the SRE
8007992These data, therefore, indicate that hyperphosphorylation of SRF plays a role in altering the ability of this protein to bind to DNA and regulate gene expression in senescent cells
Entries Per Page
Displaying Page of