The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004736 Q96CW1 AP2M1
AP2M1_HUMAN
151 157 KEEQSQITSQVTGQIGWRRE TP --- Homo sapiens (Human) 435

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0004 affinity chromatography technology in vivo/in vitro Ricotta,2002 support certain InteractionDetection
experimental MI:0424 protein kinase assay in vitro Ricotta,2002 support certain InteractionDetection
experimental MI:0943 detection by mass spectrometry in vivo/in vitro Pu,2020 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(Q2M2I8) AAK1_HUMAN 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
46 315 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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