Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Phorbol esters and cytokines regulate the expression of the NEMO-related protein, a molecule involved in a NF-kappa B-independent pathway.
Optineurin links myosin VI to the Golgi complex and is involved in Golgi organization and exocytosis.
-
OPTN binds myosin VI (and Rab8/huntingtin) at the Golgi; its depletion fragments the Golgi, removes myosin VI from the Golgi, and reduces VSV-G exocytosis, establishing roles in Golgi ribbon formation and exocytosis.
Towards a proteome-scale map of the human protein-protein interaction network.
Huntingtin interacting proteins are genetic modifiers of neurodegeneration.
Functional dissection of Rab GTPases involved in primary cilium formation.
Enhanced binding of TBK1 by an optineurin mutant that causes a familial form of primary open angle glaucoma.
Cargo binding induces dimerization of myosin VI.
Regulation of endocytic trafficking of transferrin receptor by optineurin and its impairment by a glaucoma-associated mutant.
Optineurin negatively regulates the induction of IFNbeta in response to RNA virus infection.
A comprehensive resource of interacting protein regions for refining human transcription factor networks.
Overexpression of optineurin E50K disrupts Rab8 interaction and leads to a progressive retinal degeneration in mice.
Next-generation sequencing to generate interactome datasets.
Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth.
-
OPTN is a bona fide selective autophagy receptor that binds polyubiquitin (UBAN) and LC3/GABARAP (LIR); TBK1 phosphorylates OPTN at Ser177, enhancing LC3 affinity and autophagic clearance of cytosolic Salmonella. Loss of OPTN or TBK1, or UBAN/LIR mutations, increases bacterial proliferation.
Mapping a dynamic innate immunity protein interaction network regulating type I interferon production.
Toward an understanding of the protein interaction network of the human liver.
Optineurin mediates a negative regulation of Rab8 by the GTPase-activating protein TBC1D17.
Development and application of a DNA microarray-based yeast two-hybrid system.
A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome.
Interaction between optineurin and the bZIP transcription factor NRL.
Identification and comparative analysis of hepatitis C virus-host cell protein interactions.
Oligomerization of optineurin and its oxidative stress- or E50K mutation-driven covalent cross-linking: possible relationship with glaucoma pathology.
Ubiquitylation of autophagy receptor Optineurin by HACE1 activates selective autophagy for tumor suppression.
Optineurin is an autophagy receptor for damaged mitochondria in parkin-mediated mitophagy that is disrupted by an ALS-linked mutation.
-
OPTN is recruited (Parkin-dependently, via its UBAN domain) to ubiquitinated damaged mitochondria and recruits LC3 via its LIR to drive mitophagy; the ALS-linked UBAN mutant E478G fails to rescue, defining OPTN as a mitophagy receptor.
A proteome-scale map of the human interactome network.
Haploinsufficiency of TBK1 causes familial ALS and fronto-temporal dementia.
Widespread macromolecular interaction perturbations in human genetic disorders.
Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.
The TBK1-binding domain of optineurin promotes type I interferon responses.
A novel amyotrophic lateral sclerosis mutation in OPTN induces ER stress and Golgi fragmentation in vitro.
-
The ALS12 OPTN variant V295F increases Golgi fragmentation, decreases Golgi ribbon formation, and increases susceptibility to ER stress, without changing Golgi localization or expression level.
The Golgi apparatus acts as a platform for TBK1 activation after viral RNA sensing.
An interactome perturbation framework prioritizes damaging missense mutations for developmental disorders.
A protein-protein interaction map of the TNF-induced NF-κB signal transduction pathway.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
A reference map of the human binary protein interactome.
Kinase Interaction Network Expands Functional and Disease Roles of Human Kinases.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Global Proximity Interactome of the Human Macroautophagy Pathway.
Multimodal cell maps as a foundation for structural and functional genomics.
Interaction of an adenovirus E3 14.7-kilodalton protein with a novel tumor necrosis factor alpha-inducible cellular protein containing leucine zipper domains.
Phosphorylated OPTN translocates to the nucleus
OPTN binds polyUb-RIPK1 within the TNFR1 complex
OPTN binds TBK1 within the activated TLR4 complex
OPTN recruits CYLD to the TNFR1 complex
OPTN, TBK1 bind ubiquitinated MOM proteins
MAP1LC3B binds p-S-OPTN bound to Ub-mitochondria
TBK1 is phosphorylated within TBK1:OPTN:Ub-mitochondrial proteins
p-S-TBK1 phosphorylates OPTN
OPTN binds TBK1 within the activated TLR3 complex