The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004610 Q24564 Mer
MERH_DROME
613 618 QIKAGENKYSTLKKLKSGST TP --- Drosophila melanogaster (Fruit fly) 635

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0573 mutation disrupting interaction in vivo/in vitro Hughes,2006 support certain
experimental MI:0096 pull down in vivo/in vitro Hughes,2006 support certain InteractionDetection
experimental MI:0424 protein kinase assay in vivo Hughes,2006 support certain InteractionDetection
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Hughes,2006 support certain InteractionDetection
experimental MI:1088 phenotype-based detection assay Hughes,2006 support certain InteractionDetection
experimental MI:0788 knock out in vivo Hughes,2006 support certain

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(Q8MLP1) Q8MLP1_DROME 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
37 295 [mitab][xml]
Please cite: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
feedback@elm.eu.org