Accession | Acc. Gene-, Name | Start | End | Subsequence | Logic | PDB | Organism | Length |
---|---|---|---|---|---|---|---|---|
ELMI000453 | P49418 AMPH AMPH_HUMAN |
380 | 385 | HSPMSQTLPWDLWTTSTDLV | TP |
1UTC |
Homo sapiens (Human) | 695 |
Instance evidence
Evidence class | PSI-MI | Method | BioSource | PubMed | Logic | Reliability | Notes |
---|---|---|---|---|---|---|---|
experimental | MI:0096 | pull down | in vivo/in vitro | support | certain | InteractionDetection | |
experimental | MI:0519 | glutathione s tranferase tag | in vitro | Slepnev,2000 | support | certain | |
experimental | MI:0096 | pull down | in vivo/in vitro | support | certain | InteractionDetection | |
experimental | MI:0519 | glutathione s tranferase tag | in vitro | Miele,2004 | support | certain | |
experimental | MI:0096 | pull down | in vivo/in vitro | support | certain | InteractionDetection | |
experimental | MI:0519 | glutathione s tranferase tag | in vitro | Drake,2001 | support | certain | |
experimental | MI:0113 | western blot | in vitro | Drake,2001 | support | certain | ParticipantIdentification FeatureDetection |
experimental | MI:0074 | mutation analysis | in vivo/in vitro | Drake,2001 | support | certain | FeatureDetection |
experimental | MI:0114 | x-ray crystallography | in vitro | Miele,2004 | support | certain | InteractionDetection FeatureDetection |
experimental | MI:0017 | classical fluorescence spectroscopy | in vitro | Miele,2004 | support | certain | InteractionDetection |
experimental | MI:0074 | mutation analysis | in vivo/in vitro | Slepnev,2000 | support | certain | FeatureDetection |
Switches
This ELM instance is part of the following 2 switching mechanisms annotated at the switches.ELM resource:
-
SWTI000676:
Phosphorylation of T387 adjacent to the clathrin-binding motif of Amphiphysin (AMPH) by CK2 subfamily inhibits binding to the Clathrin heavy chain 1 (CLTC). A second clathrin-binding motif in Amphiphysin (AMPH) is regulated in a similar manner (see switch details). Both these motifs cooperate in avidity-based binding to Clathrin heavy chain 1 (CLTC) (see switch details).
-
SWTI000677:
Amphiphysin 1 contains two distinct motifs that bind to distinct sites on N-terminal beta-propeller domain of clathrin, resulting in increased binding strength to free domain. This, in combination with binding of its BAR domain to curved membranes, results in localisation of amphipysin to the periphery of the assembling clathrin lattice. The two clathrin-binding motifs are regulated by phosphorylation of adjacent modification sites (see switch details and switch details).
Pathways
KEGG: The sequence P49418 is implicated in the following 2 Pathways: (color codes: This sequence=red, interacting sequence=orange)
Please cite:
ELM-the Eukaryotic Linear Motif resource-2024 update.
(PMID:37962385)
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement