The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004884 F5HDE4 ORF45
ORF45_HHV8P
63 66 TVIDMSAPDDVFAEDTPSPP TP 7OPO  
Human herpesvirus 8 strain GK18 407

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0114 x-ray crystallography in vitro Alexa,2022 support certain InteractionDetection FeatureDetection
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Sorgeloos,2022 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(P51812) KS6A3_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
68 327 [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