The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004546 B2RUJ5 Apba1
APBA1_MOUSE
381 387 TPDEPKEPIWVMRQDISPTR TP 6LNM  
Mus musculus (House mouse) 842

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0808 comigration in sds page in vitro Wu,2020 support certain InteractionDetection
experimental MI:0416 fluorescence microscopy Wu,2020 support certain InteractionDetection
experimental MI:0065 isothermal titration calorimetry in vitro Wu,2020 support certain InteractionDetection
experimental MI:0114 x-ray crystallography in vitro Wu,2020 support certain InteractionDetection FeatureDetection
experimental MI:0113 western blot in vitro Borg,1999 support likely ParticipantIdentification FeatureDetection
experimental MI:0519 glutathione s tranferase tag in vitro Borg,1999 support likely
experimental MI:0074 mutation analysis in vivo/in vitro Borg,1999 support likely FeatureDetection
experimental MI:0096 pull down in vivo/in vitro Borg,1999 support likely InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(Q62915) CSKP_RAT 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 0.0048/0.6 [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