spacer

GO:0018279 protein N-linked glycosylation via asparagine

Term Information

ID GO:0018279
Name protein N-linked glycosylation via asparagine
Ontology Biological Process
Definition The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
GONUTS GO:0018279 Wiki Page

Synonyms

Synonyms are alternative words or phrases closely related in meaning to the term name, with indication of the relationship between the name and synonym given by the synonym scope. Click on the icon for more details.
Type Synonym
exact protein amino acid N-linked glycosylation via asparagine

Cross-references

Database ID
InterPro IPR005013

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:0018279:
Relationship To GO:0018279 Child Term Child Term Name
Is a GO:0071905 protein N-linked glucosylation via asparagine
Is a GO:0071904 protein N-linked N-acetylgalactosaminylation via asparagine
Is a GO:0071903 protein N-linked N-acetylglucosaminylation via asparagine

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:0018279. 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:0018279 based on the entire annotation set Co-occurrence statistics for GO:0018279 based on non-IEA annotations only

Change Log

All changes

Timestamp Action Category Detail
2010-10-24 Added SYNONYM protein amino acid N-linked glycosylation via asparagine
2010-10-24 Updated TERM protein N-linked glycosylation via asparagine
2010-10-15 Added DEFINITION The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-10-15 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-09-17 Added DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-09-17 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-09-17 Deleted XREF RESID:AA0151
2008-05-13 Added DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2008-05-12 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2008-04-01 Updated RELATION is a GO:0018196 (peptidyl-asparagine modification)
2008-04-01 Updated RELATION is a GO:0006487 (protein N-linked glycosylation)
2005-07-05 Updated TERM protein amino acid N-linked glycosylation via asparagine
2003-10-27 Added XREF RESID:AA0151
2003-04-24 Updated DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2002-11-27 Added DEFINITION The post-translational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-[ST] motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2001-10-01 Added TERM N-linked glycosylation via asparagine

Term

Timestamp Action Category Detail
2010-10-24 Updated TERM protein N-linked glycosylation via asparagine
2005-07-05 Updated TERM protein amino acid N-linked glycosylation via asparagine
2001-10-01 Added TERM N-linked glycosylation via asparagine

Definition/synonyms

Timestamp Action Category Detail
2010-10-24 Added SYNONYM protein amino acid N-linked glycosylation via asparagine
2010-10-15 Added DEFINITION The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-10-15 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-09-17 Added DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2010-09-17 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2008-05-13 Added DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2008-05-12 Deleted DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2003-04-24 Updated DEFINITION The posttranslational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.
2002-11-27 Added DEFINITION The post-translational glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine also occurs; this modification typically occurs in extracellular peptides with an N-X-[ST] motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

Relationships

Timestamp Action Category Detail
2008-04-01 Updated RELATION is a GO:0018196 (peptidyl-asparagine modification)
2008-04-01 Updated RELATION is a GO:0006487 (protein N-linked glycosylation)

Cross-references

Timestamp Action Category Detail
2010-09-17 Deleted XREF RESID:AA0151
2003-10-27 Added XREF RESID:AA0151
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.
14ms