The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004533 Q8N137 CNTROB
CNTRB_HUMAN
38 44 SEVTSQLYASLRLSRQAEAT TP --- Homo sapiens (Human) 903

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0113 western blot in vitro Park,2013 support certain ParticipantIdentification FeatureDetection
experimental MI:0413 electrophoretic mobility shift assay Park,2013 support certain InteractionDetection
experimental MI:0005 alanine scanning in vivo/in vitro/in silico Park,2013 support certain FeatureDetection
experimental MI:0424 protein kinase assay in vitro Park,2013 support certain InteractionDetection
experimental MI:0424 protein kinase assay in vivo Park,2013 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(P51955) NEK2_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
8 271 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
feedback@elm.eu.org