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PMID:10081969
| Citation |
Tanahashi, H and Tabira, T (1999) Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein. Neurosci. Lett. 261:143-6 |
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| Abstract |
We report the cDNA sequence of human Fe65L2. The human Fe65L2 encoded 486 amino acids; the deduced amino acid sequence was shorter by 18 amino acids than the rat protein and had 86% identity to the rat protein Three protein-protein interaction domains, a WW and two PID/PTB elements, were conserved among the Fe65 protein family. Human Fe65L2 mRNA was expressed in various tissues; a transcript of about 2.2 kb was mainly expressed in the brain. A splicing variant lacking two amino acids in the first PID/PTB element was detected. We also confirmed that the carboxyl-terminal region of PID/PTB of the Fe65L2 interacted with the intracellular domain of the Alzheimer's beta-amyloid precursor protein (APP) and APP-like proteins. |
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| Keywords |
Alzheimer Disease/metabolism; Amino Acid Sequence; Amyloid beta-Protein Precursor/biosynthesis; Amyloid beta-Protein Precursor/metabolism; Animals; Base Sequence; Blotting, Northern; Carrier Proteins/biosynthesis; Carrier Proteins/metabolism; Cloning, Molecular; DNA, Complementary/biosynthesis; Humans; Molecular Sequence Data; Phosphoproteins/biosynthesis; Phosphoproteins/metabolism; RNA, Messenger/biosynthesis; Rats |
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Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
|
HUMAN:APBB3 |
located_in |
GO:0005737: cytoplasm |
ECO:0000304: author statement supported by traceable reference used in manual assertion |
C |
Seeded From UniProt |
complete | ||
|
HUMAN:APBB3 |
enables |
GO:0005515: protein binding |
ECO:0000353: physical interaction evidence used in manual assertion |
UniProtKB:P05067 |
F |
Seeded From UniProt |
complete | |
|
enables |
GO:0005515: protein binding |
ECO:0000353: physical interaction evidence used in manual assertion |
UniProtKB:O95704 |
F |
Seeded From UniProt |
complete | ||
See also
References
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