Pub. Date : 2000 Sep 29
PMID : 10889209
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | Both GIRK1 and GIRK4 have one extracellular consensus N-glycosylation site. | Nitrogen | potassium inwardly rectifying channel subfamily J member 3 | Homo sapiens |
| 2 | GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site. | Asparagine | potassium inwardly rectifying channel subfamily J member 3 | Homo sapiens |
| 3 | GIRK1 membrane-spanning domain 1 was required for optimal glycosylation at Asn(119) because a chimera that contained GIRK4 membrane-spanning domain 1 significantly reduced the addition of a carbohydrate structure at this site. | Carbohydrates | potassium inwardly rectifying channel subfamily J member 3 | Homo sapiens |
| 4 | Thus, N-glycosylation of GIRK1 at Asn(119) does not appear to affect its physical association with GIRK4, the routing of the heteromer to the cell surface, or heteromeric channel function, unlike the dramatic functional effects of N-glycosylation of ROMK1 at Asn(117) (Schwalbe, R. A., Wang, Z., Wible, B. | Asparagine | potassium inwardly rectifying channel subfamily J member 3 | Homo sapiens |