The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004607 P15311 EZR
564 569 NMRQGRDKYKTLRQIRQGNT TP --- Homo sapiens (Human) 586

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0421 identification by antibody Zaman,2021 support certain ParticipantIdentification
experimental MI:0573 mutation disrupting interaction in vivo/in vitro Zaman,2021 support certain
experimental MI:1088 phenotype-based detection assay Zaman,2021 support certain InteractionDetection
experimental MI:0788 knock out in vivo Zaman,2021 support certain
predicted MI:0101 sequence based prediction in silico Belkina,2009 support likely InteractionDetection
predicted MI:0403 colocalization in vitro Belkina,2009 support likely
experimental MI:0403 colocalization in vitro Pelaseyed,2017 support certain
experimental MI:0424 protein kinase assay in vitro Pelaseyed,2017 support certain InteractionDetection

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]

o  Pathways

KEGG: The sequence P15311 is implicated in the following 7 Pathways: (color codes: This sequence=red, interacting sequence=orange)
Please cite: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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