HCSGD entry for MAP1LC3A


1. General information

Official gene symbolMAP1LC3A
Entrez ID84557
Gene full namemicrotubule-associated protein 1 light chain 3 alpha
Other gene symbolsATG8E LC3 LC3A MAP1ALC3 MAP1BLC3
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:0000045Autophagic vacuole assemblyISSbiological_process
GO:0000421Autophagic vacuole membraneIEAcellular_component
GO:0000422Mitochondrion degradationIGIbiological_process
GO:0005515Protein bindingIPImolecular_function
GO:0005543Phospholipid bindingIDAmolecular_function
GO:0005770Late endosomeIEAcellular_component
GO:0005776Autophagic vacuoleIDAcellular_component
GO:0005829CytosolIDAcellular_component
GO:0005874MicrotubuleIEAcellular_component
GO:0008429Phosphatidylethanolamine bindingIDAmolecular_function
GO:0012505Endomembrane systemIEAcellular_component
GO:0031090Organelle membraneIDAcellular_component
GO:0031410Cytoplasmic vesicleIEAcellular_component
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4. Expression levels in datasets

  • Meta-analysis result

p-value upp-value downFDR upFDR down
0.53320194900.04729171380.99999024730.4079859718

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

Data sourceUp or downLog fold change
GSE11954Down-0.0783269703
GSE13712_SHEARDown-0.5913238802
GSE13712_STATICDown-0.4170635976
GSE19018Up0.3443504098
GSE19899_A1Down-1.3025050061
GSE19899_A2Down-0.4571594761
PubMed_21979375_A1Down-0.1248681234
PubMed_21979375_A2Down-0.7700582870
GSE35957Up0.7144945187
GSE36640Up0.3887400213
GSE54402Down-0.1705441918
GSE9593Up0.6843584272
GSE43922Down-0.5801875520
GSE24585Down-0.1291495949
GSE37065Up0.0605828278
GSE28863_A1Up0.0237839272
GSE28863_A2Down-0.3553734617
GSE28863_A3Up0.2085967109
GSE28863_A4Down-0.1056311331
GSE48662Up0.6656105740

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-335-5pMIMAT0000765MIRT018831MicroarrayFunctional 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: 12 abstracts the gene occurs.


PubMed ID of the article

Sentenece the gene occurs

26930622We evaluated cell toxicity, apoptosis, viability, proliferation, senescence and autophagy in response to APAP (acetaminophen), cisplatin, dexamethasone, gentamicin, penicillin, neomycin, streptomycin, and tobramycin, at five different doses and two time-points (24 and 48 h), by flow cytometry techniques and caspase 3/7, MTT, Cytotoxicity, BrdU, Beclin1, LC3 and SA-beta-galactosidase assays
26654219We reveal that the autophagy protein LC3/Atg8 directly interacts with the nuclear lamina protein LMNB1 (lamin B1), and binds to LMN/lamin-associated chromatin domains (LADs)
26035971Since cell senescence process may be associated with changes in autophagy regulation, we analyzed the dynamics of one of the main autophagosome formation markers--protein LC3
25440825Autophagy was evaluated by image analysis techniques for the expression of light chain 3 (LC3) after immunohistochemical staining of LC3 rabbit polyclonal antibody and Western blot analysis; additionally, myocyte apoptosis was determined using terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL) assay, 4',6-diamidino-2-phenylindole staining, and p53 immunohistochemical staining
25440825RESULTS: LC3 expression was significantly increased at the renal pelvis (P <
25440825A significant negative correlation was found between TUNEL and LC3 in all sections of the obstructed UPJ complex (P <
25440825Proliferating cell nuclear antigen and LC3 were positively correlated in the renal pelvis and UPJ (P <
25186470Knockdown of FOXO1 and FOXO1+3 resulted in significant reductions in levels of glutathione peroxidase 1 (GPX-1), catalase, light chain 3 (LC3), Beclin1, and sirtuin 1 (SIRT-1) proteins following treatment with tBHP
25186470In contrast, the constitutive active form of FOXO3 increased cell viability while inducing GPX-1, Beclin1, and LC3 in response to tBHP
25087910Autophagy in cells was examined by detecting for LC3, Beclin-1, m-TOR, and p70S6K, as well as by analyzing autophagosomes
23231002The granular expression of mitochondrial antigens was colocalized with LC3 in damaged SBDs in PBC
22613224Moreover, the senescence of HCT116 cells was accompanied by autophagy, that was confirmed by electron microscopy observations of autophagosomes in the curcumin-treated cells as well as LC3-II expression, punctue staining of LC3 and increased content of acidic vacuoles
21989821RESULTS: The expression of LC3 was seen in coarse vesicles in the cytoplasm of bile ductular cells and significantly more frequently in PBC of both early and advanced stages when compared to control livers (p < 0
20212459We examined immunohistochemically the expression of microtubule-associated proteins-light chain 3beta (LC3), a marker of autophagy, in livers taken from the patients with PBC (n=37) and control livers (n=75)
20212459The expression of LC3 was specifically seen in vesicles in BECs in the inflamed and damaged small bile ducts in PBC, when compared with non-inflamed small bile ducts in PBC and in control livers (P<0
20212459The expression of LC3 was closely related to the expression of cathepsin D, LAMP-1, and senescent markers
18203850The cleaved microtubule-associated protein 1 light-chain 3 (LC3), a marker of autophagosome formation, was overexpressed within 24 h of GC treatment; however, by 4-5 days, it was nearly undetectable
17635673Instead, we identified several indications of autophagy: electron microscopy showed typical autophagic vacuoles; acridine orange staining revealed acidic vesicular organelles; acidification of acidic vesicular organelles was prevented using bafilomycin A1; cells displayed arrest in G2/M; increased processing of LC3 occurred; vacuolation was prevented by the autophagy inhibitor 3-methyladenine; no caspase activation was detected
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