The Eukaryotic Linear Motif resource for
Functional Sites in Proteins

o  Instance

Accession Acc. Gene-, NameStartEndSubsequenceLogic PDB OrganismLength
ELMI004921 B8XX90 STING1
STING_PIG
368 376 EPELLISGMEQPLPLRSDIF TP --- Sus scrofa (Pig) 378

o  Instance evidence

Evidence classPSI-MIMethodBioSourcePubMedLogicReliabilityNotes
experimental MI:0403 colocalization in vitro Luo,2023 support likely
experimental MI:0119 mutation decreasing interaction in vivo/in vitro Luo,2023 support likely InteractionDetection
experimental MI:0019 coimmunoprecipitation in vivo/in vitro Luo,2023 support likely InteractionDetection

o  Interactions

Uniprot Id Domain family Domain Start Domain End Affinity Min/Max (µMol) Notes
(A0A8D1B5F0) A0A8D1B5F0_PIG 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
9 310 [mitab][xml]
(A0A8D1B5F0) A0A8D1B5F0_PIG IPR041309 (TANK-binding kinase 1, coiled-coil domain 1)
This is a coiled-coil domain found in TANK-binding kinase 1 (TBK1), it comprises one of two coiled-coil domains found in the scaffold dimerization region
400 655 [mitab][xml]
Please cite: ELM-the Eukaryotic Linear Motif resource-2024 update. (PMID:37962385)

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