Preferred Name | obsolete regulation of molecular function, epigenetic | |
Synonyms |
regulation of protein activity, epigenetic |
|
Definitions |
OBSOLETE. Any heritable epigenetic process that modulates the frequency, rate or extent of protein function by self-perpetuating conformational conversions of normal proteins in healthy cells. This is distinct from, though mechanistically analogous to, disease states associated with prion propagation and amyloidogenesis. A single protein, if it carries a glutamine/asparagine-rich ('prion') domain, can sometimes stably exist in at least two distinct physical states, each associated with a different phenotype; propagation of one of these traits is achieved by a self-perpetuating change in the protein from one form to the other, mediated by conformational changes in the glutamine/asparagine-rich domain. Prion domains are both modular and transferable to other proteins, on which they can confer a heritable epigenetic alteration of function; existing bioinformatics data indicate that they are rare in non-eukarya, but common in eukarya. This term was obsoleted because it is not an active process. |
|
ID |
http://purl.obolibrary.org/obo/GO_0040030 |
|
Obsolete |
true |
|
comment |
This term was obsoleted because it is not an active process. |
|
definition |
OBSOLETE. Any heritable epigenetic process that modulates the frequency, rate or extent of protein function by self-perpetuating conformational conversions of normal proteins in healthy cells. This is distinct from, though mechanistically analogous to, disease states associated with prion propagation and amyloidogenesis. A single protein, if it carries a glutamine/asparagine-rich ('prion') domain, can sometimes stably exist in at least two distinct physical states, each associated with a different phenotype; propagation of one of these traits is achieved by a self-perpetuating change in the protein from one form to the other, mediated by conformational changes in the glutamine/asparagine-rich domain. Prion domains are both modular and transferable to other proteins, on which they can confer a heritable epigenetic alteration of function; existing bioinformatics data indicate that they are rare in non-eukarya, but common in eukarya. |
|
deprecated |
true |
|
has_exact_synonym |
regulation of protein activity, epigenetic |
|
has_obo_namespace |
biological_process |
|
id |
GO:0040030 |
|
label |
obsolete regulation of molecular function, epigenetic |
|
notation |
GO:0040030 |
|
prefLabel |
obsolete regulation of molecular function, epigenetic |
|
term tracker item |
Delete | Mapping To | Ontology | Source |
---|---|---|---|
http://purl.obolibrary.org/obo/GO_0040030 | GO-EXT | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | ONE | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | OBI_BCGO | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | EGO | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | PHAGE | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | GO-PLUS | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | BERO | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | OBI_IEE | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | FTC | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | NIFSTD | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | GO | SAME_URI | |
http://purl.obolibrary.org/obo/GO_0040030 | PHAGE | LOOM | |
http://purl.obolibrary.org/obo/GO_0040030 | GO-PLUS | LOOM | |
http://purl.obolibrary.org/obo/GO_0040030 | BERO | LOOM | |
http://purl.obolibrary.org/obo/GO_0040030 | NIFSTD | LOOM | |
http://purl.obolibrary.org/obo/GO_0040030 | GO | LOOM |