spacer

GO:0016975 alpha-2 macroglobulin

This term is obsolete.
This term was made obsolete because it represents a gene product.

Term Information

ID GO:0016975
Name alpha-2 macroglobulin
Ontology Molecular Function
Definition OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
Comment This term was made obsolete because it represents a gene product.
GONUTS GO:0016975 Wiki Page

Replaced by

This term is obsolete - try one of these terms:
Advice GO Identifier Ontology GO Term Name
Replaced by GO:0004866 Molecular Function endopeptidase inhibitor activity

Ancestor Chart

This chart is interactive; you can click on the term boxes and legend for more information.
Display options
Display
Key
GO IDs
Term box width
Term box height
Slim colours
Show children
Image size limit (in megapixels)
Note that setting the limit too high may result in images being generated slowly; it may even cause the browser to crash. The maximum limit is 20 megapixels.

Child Terms

This table lists all terms that are direct descendants (child terms) of GO:0016975:
Term has no children

Protein Annotation

Displaying annotations FIRST to LAST of TOTAL Page size: Additional filters: Bookmarkable link
Database
Gene Product ID
Symbol
Qualifier
GO Identifier
GO Term Name
Aspect
Original GO ID
Original GO Term Name
Evidence
Reference
With
Taxon
Date
Assigned By
Product Form ID
Name
Synonym
Type
Taxon Name
Sequence

Export

Display options

ID Mapping

QuickGO maps between different identifier types by using a combination of mapping files provided by the databases, and using identifier cross-references supplied by UniProtKB.

If more than one identifier type needs to be used to map all required sequences, drag the selected databases to change the order in which identifiers are found.

Filter

Select

Grouped by
Annotation count
Protein count
Both

Co-occurring Terms

These tables show the number of times the term listed in the table has been co-annotated with GO:0016975. The terms are listed in descending order of number of times the term has been co-annotated.
The table on the left is calculated using both electronic and manual-evidenced annotations, while the table on the right is calculated using only manual-evidenced annotations.
Co-occurrence statistics for GO:0016975 based on the entire annotation set Co-occurrence statistics for GO:0016975 based on non-IEA annotations only

Change Log

All changes

Timestamp Action Category Detail
2010-06-08 Deleted RELATION is a GO:0008369 (obsolete molecular function)
2010-06-08 Updated TERM alpha-2 macroglobulin
2008-06-03 Added OBSOLETION replaced_by GO:0004866 (endopeptidase inhibitor activity)
2008-05-13 Added DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2008-05-12 Deleted DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2008-04-01 Updated RELATION is a GO:0008369 (obsolete molecular function)
2003-03-26 Updated DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2002-11-27 Updated DEFINITION Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2002-07-09 Updated TERM alpha-2 macroglobulin
2002-02-06 Updated TERM alpha2-macroglobulin
2001-08-06 Added DEFINITION Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiol-ester bond is hydrolysed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiol-ester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2001-04-03 Updated TERM alpha2-macroglobulin
2001-03-30 Added TERM alpha2-macroglobulin

Term

Timestamp Action Category Detail
2010-06-08 Updated TERM alpha-2 macroglobulin
2002-07-09 Updated TERM alpha-2 macroglobulin
2002-02-06 Updated TERM alpha2-macroglobulin
2001-04-03 Updated TERM alpha2-macroglobulin
2001-03-30 Added TERM alpha2-macroglobulin

Obsoletions

Timestamp Action Category Detail
2008-06-03 Added OBSOLETION replaced_by GO:0004866 (endopeptidase inhibitor activity)

Definition/synonyms

Timestamp Action Category Detail
2008-05-13 Added DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2008-05-12 Deleted DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2003-03-26 Updated DEFINITION OBSOLETE. Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2002-11-27 Updated DEFINITION Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiolester bond is hydrolyzed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiolester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.
2001-08-06 Added DEFINITION Inhibition of proteinase by a mechanism involving a bait region which contains specific sites, cleavage of which induces a conformational change that results in trapping of the proteinase; following cleavage in the bait region a thiol-ester bond is hydrolysed and mediates the covalent binding of the protein to the proteinase; subsequently epsilon-amino groups of the proteinase react with thiol-ester linkages in the inhibitor to form stable amide links; the entrapped proteinase can now only act on low molecular mass substrates.

Relationships

Timestamp Action Category Detail
2010-06-08 Deleted RELATION is a GO:0008369 (obsolete molecular function)
2008-04-01 Updated RELATION is a GO:0008369 (obsolete molecular function)
spacer
Please send comments, suggestions or bug reports to goa@ebi.ac.uk. Click here for details of how to cite UniProt-GOA and QuickGO.
12ms