The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004722 P32521 PAN1
393 399 TAGVQNLQPQPTGYMPQTSF TP --- Saccharomyces cerevisiae S288c 1480

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0101 sequence based prediction in silico Zeng,1999 support certain InteractionDetection
experimental MI:0818 molecular weight estimation by coomasie staining Zeng,1999 support certain ParticipantIdentification
experimental MI:0833 autoradiography Zeng,1999 support certain ParticipantIdentification FeatureDetection
experimental MI:0506 over expressed level in vivo Zeng,1999 support certain
experimental MI:0519 glutathione s tranferase tag in vitro Zeng,1999 support certain
experimental MI:0424 protein kinase assay in vitro Zeng,1999 support certain InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(P40494) PRK1_YEAST 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
22 298 [mitab][xml]
Please cite: The Eukaryotic Linear Motif resource: 2022 release. (PMID:34718738)

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