ELM - instance MOD_AAK1BIKe_LxxQxTG_1 in sequence P32521 at position 565

The Eukaryotic Linear Motif resource for

Functional Sites in Proteins

MOD_AAK1BIKe_LxxQxTG_1

Instance

Accession	Acc. Gene-, Name	Start	End	Subsequence	Logic	PDB	Organism	Length
ELMI004730	P32521 PAN1 PAN1_YEAST	565	571	FSATMPLTAQKTGFGNNEIY	TP	---	Saccharomyces cerevisiae S288c	1480

Instance evidence

Evidence class	PSI-MI	Method	BioSource	PubMed	Logic	Reliability	Notes
experimental	MI:0101	sequence based prediction	in silico	Zeng,1999	support	certain	InteractionDetection
experimental	MI:0083	peptide synthesis		Zeng,1999	support	certain	ParticipantIdentification
experimental	MI:0818	molecular weight estimation by coomasie staining		Zeng,1999	support	certain	ParticipantIdentification
experimental	MI:0833	autoradiography		Zeng,1999	support	certain	ParticipantIdentification FeatureDetection
experimental	MI:0573	mutation disrupting interaction	in vivo/in vitro	Zeng,1999	support	certain
experimental	MI:0074	mutation analysis	in vivo/in vitro	Zeng,1999	support	certain	FeatureDetection
experimental	MI:0506	over expressed level	in vivo	Zeng,1999	support	certain
experimental	MI:0519	glutathione s tranferase tag	in vitro	Zeng,1999	support	certain
experimental	MI:0424	protein kinase assay	in vitro	Zeng,1999	support	certain	InteractionDetection

Interactions

Uniprot Id	Domain family	Domain Start	Domain End	Affinity Min/Max (µMol)	Notes
(P40494) PRK1_YEAST	IPR000719 (Protein kinase domain) Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases	22	298		[mitab][xml]

Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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