ELM - instance LIG_Clathr_ClatBox_2 in sequence P49418 at position 380

Instance

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: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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