The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004551 O75334 PPFIA2
LIPA2_HUMAN
977 984 PTSRTPSGNVWVTHEEMENL TP 3TAC  
Homo sapiens (Human) 1257

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0004 affinity chromatography technology in vivo/in vitro Wei,2011 support likely InteractionDetection
experimental MI:0416 fluorescence microscopy Wei,2011 support likely InteractionDetection
experimental MI:0065 isothermal titration calorimetry in vitro Wei,2011 support likely InteractionDetection
experimental MI:0114 x-ray crystallography in vitro Wei,2011 support likely InteractionDetection FeatureDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(O14936) CSKP_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
12 276 0.6/0.6 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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