The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004532 Q92997 DVL3
DVL3_HUMAN
640 646 HRSHHSLASSLRSHHTHPSY TP --- Homo sapiens (Human) 716

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0113 western blot in vitro Cervenka,2016 support certain ParticipantIdentification FeatureDetection
experimental MI:0424 protein kinase assay in vitro Cervenka,2016 support certain InteractionDetection
experimental MI:0427 Identification by mass spectrometry Cervenka,2016 support certain ParticipantIdentification
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Cervenka,2016 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(P51955) NEK2_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
8 271 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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