The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004606 P26038 MSN
MOES_HUMAN
555 560 NMRLGRDKYKTLRQIRQGNT TP --- Homo sapiens (Human) 577

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0788 knock out in vivo Belkina,2009 support certain
experimental MI:1088 phenotype-based detection assay Belkina,2009 support certain InteractionDetection
experimental MI:0424 protein kinase assay in vivo Belkina,2009 support certain InteractionDetection
experimental MI:0081 peptide array Belkina,2009 support certain InteractionDetection
experimental MI:0424 protein kinase assay in vitro Belkina,2009 support certain InteractionDetection
experimental MI:0403 colocalization in vitro Belkina,2009 support certain

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(O94804) STK10_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
36 294 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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