The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004733 O13736 sla1
SLA1_SCHPO
1118 1124 MPQMTGVQVQKTGAMPQQPV TP --- Schizosaccharomyces pombe 972h- 1420

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0101 sequence based prediction in silico Zeng,2001 support certain InteractionDetection
experimental MI:0413 electrophoretic mobility shift assay Zeng,2001 support certain InteractionDetection
experimental MI:0416 fluorescence microscopy Zeng,2001 support certain InteractionDetection
experimental MI:0091 chromatography technology in vitro Zeng,2001 support certain InteractionDetection
experimental MI:0018 two hybrid in vivo Zeng,2001 support certain InteractionDetection
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Zeng,2001 support certain InteractionDetection
experimental MI:0519 glutathione s tranferase tag in vitro Zeng,2001 support certain
experimental MI:0424 protein kinase assay in vitro Zeng,2001 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(P40494) PRK1_YEAST 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
22 298 [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