The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004608 P35241 RDX
561 566 NVKAGRDKYKTLRQIRQGNT TP --- Homo sapiens (Human) 583

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

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: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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