The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004548 Q8WXD9 CASKIN1
CSKI1_HUMAN
374 379 GPSAPPEEIWVLRKPFAGGD TP --- Homo sapiens (Human) 1431

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0807 comigration in gel electrophoresis in vitro Stafford,2011 support certain InteractionDetection
experimental MI:0071 molecular sieving in vivo/in vitro Stafford,2011 support certain InteractionDetection
experimental MI:0405 competition binding in vitro Stafford,2011 support certain InteractionDetection
experimental MI:0005 alanine scanning in vivo/in vitro/in silico Stafford,2011 support certain FeatureDetection
experimental MI:0074 mutation analysis in vivo/in vitro Stafford,2011 support certain FeatureDetection
experimental MI:0107 surface plasmon resonance in vitro Stafford,2011 support certain 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 7.0/8.0 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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