Name
Tay-Sachs Disease
Annospace Keyword
MeSHDisease
Annospace Name
MeSH
Annospace Version
20170511
Annospace URL
https://arty.scai.fraunhofer.de/artifactory/bel/annotation/mesh-diseases/mesh-diseases-20170511.belanno

Sample Edges 5

p(HGNC:HEXA) directlyDecreases act(p(HGNC:HEXA), ma(cat))

The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive. It was found to be improperly folded into an insoluble aggregate, linked through inappropriate disulfide bonds. The unglycosylated protein was trapped in the lumen of the endoplasmic reticulum and was found in a complex with the Ig heavy chain-binding protein, BiP. The properties of the nonglycosylated, misfolded alpha-subunit were similar to some mutant alpha-subunits in Tay-Sachs disease patients. PubMed:1533633

Annotations
NCBI Taxonomy Ids
9606
Experimental Factor Ontology (EFO)
COS-1 cell
Disease Ontology (DO)
colorectal cancer
MeSH
Tay-Sachs Disease

p(HGNC:HEXA) directlyDecreases act(p(HGNC:HEXA), ma(chap))

The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive. It was found to be improperly folded into an insoluble aggregate, linked through inappropriate disulfide bonds. The unglycosylated protein was trapped in the lumen of the endoplasmic reticulum and was found in a complex with the Ig heavy chain-binding protein, BiP. The properties of the nonglycosylated, misfolded alpha-subunit were similar to some mutant alpha-subunits in Tay-Sachs disease patients. PubMed:1533633

Annotations
NCBI Taxonomy Ids
9606
Experimental Factor Ontology (EFO)
COS-1 cell
Disease Ontology (DO)
colorectal cancer
MeSH
Tay-Sachs Disease

p(HGNC:HEXA) directlyDecreases tloc(p(HGNC:HEXA), fromLoc(GOCC:"endoplasmic reticulum"), toLoc(GOCC:lysosome))

The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive. It was found to be improperly folded into an insoluble aggregate, linked through inappropriate disulfide bonds. The unglycosylated protein was trapped in the lumen of the endoplasmic reticulum and was found in a complex with the Ig heavy chain-binding protein, BiP. The properties of the nonglycosylated, misfolded alpha-subunit were similar to some mutant alpha-subunits in Tay-Sachs disease patients. PubMed:1533633

Annotations
NCBI Taxonomy Ids
9606
Experimental Factor Ontology (EFO)
COS-1 cell
Disease Ontology (DO)
colorectal cancer
MeSH
Tay-Sachs Disease

p(HGNC:HEXA) association path(MESHD:"Tay-Sachs Disease")

The unglycosylated alpha-subunit, resulting from genetic alteration of all three glycosylation sites or synthesis of the wild-type protein in the presence of tunicamycin, was catalytically inactive. It was found to be improperly folded into an insoluble aggregate, linked through inappropriate disulfide bonds. The unglycosylated protein was trapped in the lumen of the endoplasmic reticulum and was found in a complex with the Ig heavy chain-binding protein, BiP. The properties of the nonglycosylated, misfolded alpha-subunit were similar to some mutant alpha-subunits in Tay-Sachs disease patients. PubMed:1533633

Annotations
NCBI Taxonomy Ids
9606
Experimental Factor Ontology (EFO)
COS-1 cell
Disease Ontology (DO)
colorectal cancer
MeSH
Tay-Sachs Disease

bp(GOBP:transport) association p(HGNC:HEXA, pmod(Glyco))

We have identified the sites of N-linked glycosylation and oligosaccharide phosphorylation on the alpha-subunit of beta-hexosaminidase and have determined the influence of the oligosaccharides on the folding and transport of the enzyme. PubMed:1533633

Annotations
NCBI Taxonomy Ids
9606
Experimental Factor Ontology (EFO)
COS-1 cell
Disease Ontology (DO)
colorectal cancer
MeSH
Tay-Sachs Disease

About

BEL Commons is developed and maintained in an academic capacity by Charles Tapley Hoyt and Daniel Domingo-Fernández at the Fraunhofer SCAI Department of Bioinformatics with support from the IMI project, AETIONOMY. It is built on top of the open source project, PyBEL. Please feel free to contact us here to give us feedback or report any issues.