HCSGD entry for SERPINA1


1. General information

Official gene symbolSERPINA1
Entrez ID5265
Gene full nameserpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 1
Other gene symbolsA1A A1AT AAT PI PI1 PRO2275 alpha1AT
Links to Entrez GeneLinks to Entrez Gene

2. Neighbors in the network

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This gene isn't in Literature mining network.

3. Gene ontology annotation

GO ID

GO term

Evidence

Category

GO:0002020Protease bindingIPImolecular_function
GO:0002576Platelet degranulationTASbiological_process
GO:0004867Serine-type endopeptidase inhibitor activityIDA NASmolecular_function
GO:0005515Protein bindingIPImolecular_function
GO:0005576Extracellular regionNAS TAScellular_component
GO:0005578Proteinaceous extracellular matrixIEAcellular_component
GO:0005615Extracellular spaceIDA IEA IMPcellular_component
GO:0005783Endoplasmic reticulumIDAcellular_component
GO:0006953Acute-phase responseIEAbiological_process
GO:0007596Blood coagulationTASbiological_process
GO:0010951Negative regulation of endopeptidase activityIBAbiological_process
GO:0030162Regulation of proteolysisIBAbiological_process
GO:0030168Platelet activationTASbiological_process
GO:0031093Platelet alpha granule lumenTAScellular_component
GO:0042802Identical protein bindingIPImolecular_function
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.00770311920.95203392730.22806951631.0000000000

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

Data sourceUp or downLog fold change
GSE11954Down-0.0450350299
GSE13712_SHEARDown-0.0026163508
GSE13712_STATICDown-0.0036888568
GSE19018Up0.3556030751
GSE19899_A1Up0.4719187344
GSE19899_A2Up1.2986926893
PubMed_21979375_A1Up1.8160193502
PubMed_21979375_A2Up1.2820989434
GSE35957Up0.1724568339
GSE36640Down-0.0121573504
GSE54402Up1.8698561544
GSE9593Up0.2819379002
GSE43922Up0.7350436393
GSE24585Down-0.1133587664
GSE37065Down-0.2246628744
GSE28863_A1Down-0.0797379298
GSE28863_A2Down-0.0740724985
GSE28863_A3Up0.3689285072
GSE28863_A4Down-0.1531260668
GSE48662Up0.0403775250

5. Regulation relationships with compounds/drugs/microRNAs

  • Compounds

Not regulated by compounds

  • Drugs

Name

Drug

Accession number

2-[3,4-Dihydroxy-2-Hydroxymethyl-5-(2-Hydroxy-Nonyl)-Tetrahydro-Furan-2-Yloxy]-6-Hydroxymethyl-Tetra Hydro-Pyran-3,4,5-TriolDB01998 EXPT02980
Beta-MercaptoethanolDB03345 EXPT02882 | DB03131
Recombinant alpha 1-antitrypsinDB05481 -

  • MicroRNAs

  • mirTarBase

MiRNA_name

mirBase ID

miRTarBase ID

Experiment

Support type

References (Pubmed ID)

hsa-miR-335-5pMIMAT0000765MIRT016814MicroarrayFunctional MTI (Weak)18185580
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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: 2 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

25341065RATIONALE: alpha1-Antitrypsin (A1AT) was identified as a plasma protease inhibitor; however, it is now recognized as a multifunctional protein that modulates immunity, inflammation, proteostasis, apoptosis, and cellular senescence
25341065Like A1AT, protein phosphatase 2A (PP2A), a major serine-threonine phosphatase, regulates similar biologic processes and plays a key role in chronic obstructive pulmonary disease
25341065OBJECTIVES: Given their common effects, this study investigated whether A1AT acts via PP2A to alter tumor necrosis factor (TNF) signaling, inflammation, and proteolytic responses in this disease
25341065PP2A activation was assessed in human neutrophils, airway epithelial cells, and peripheral blood monocytes treated with plasma purified A1AT protein
25341065Similarly, lung PP2A activity was measured in mice administered intranasal A1AT
25341065PP2A was silenced in lung epithelial cells treated with A1AT and matrix metalloproteinase and cytokine production was then measured following TNF-alpha stimulation
25341065A1AT protein activated PP2A in human alveolar macrophages, monocytes, neutrophils, airway epithelial cells, and in mouse lungs
25341065This activation required functionally active A1AT protein and protein tyrosine phosphatase 1B expression
25341065CONCLUSIONS: Together, these data indicate that A1AT modulates PP2A to counter inflammatory and proteolytic responses induced by TNF signaling in the lung
22697349Systemic deficiency in AAT (AATD) due to genetic mutations can result in liver failure and chronic lung disease such as emphysema
22697349Over the past decade, however, investigations of AATD have described multiple functions of AAT beyond those generally attributed to its antiprotease activity
22697349Evidence now suggests that AAT plays an important role in modulating immunity, inflammation, proteostasis, apoptosis, and possibly cellular senescence programs
22697349Finally, we consider the data regarding treatment of AATD, including AAT supplementation and its current limitations, and suggest further avenues of research informed by the multiple functions of AAT
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