Harmonizome 3.0

LON peptidase N-terminal domain and ring finger 2 pseudogene

lon peptidase 2, peroxisomal

In human, peroxisomes function primarily to catalyze fatty acid beta-oxidation and, as a by-product, produce hydrogen peroxide and superoxide. The protein encoded by this gene is an ATP-dependent protease that likely plays a role in maintaining overall peroxisome homeostasis as well as proteolytically degrading peroxisomal proteins damaged by oxidation. The protein has an N-terminal Lon N substrate recognition domain, an ATPase domain, a proteolytic domain, and, in some isoforms, a C-terminal peroxisome targeting sequence. Alternative splicing results in multiple transcript variants encoding distinct isoforms. [provided by RefSeq, Jan 2017]

lon peptidase 1, mitochondrial

This gene encodes a mitochondrial matrix protein that belongs to the Lon family of ATP-dependent proteases. This protein mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides in the mitochondrial matrix. It may also have a chaperone function in the assembly of inner membrane protein complexes, and participate in the regulation of mitochondrial gene expression and maintenance of the integrity of the mitochondrial genome. Decreased expression of this gene has been noted in a patient with hereditary spastic paraplegia (PMID:18378094). Alternatively spliced transcript variants have been found for this gene. [provided by RefSeq, Feb 2013]

LON peptidase N-terminal domain and ring finger 2 pseudogene 2

LON peptidase N-terminal domain and ring finger 2 pseudogene 1

LON peptidase N-terminal domain and ring finger 3

The protein encoded by this gene contains a RING finger domain, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions. Multiple alternatively spliced transcript variants have been suggested, but their full length natures are not clear. [provided by RefSeq, Jul 2008]

LON peptidase N-terminal domain and ring finger 2

Predicted to enable ubiquitin protein ligase activity. Predicted to be located in cytoplasm. [provided by Alliance of Genome Resources, Mar 2025]

LON peptidase N-terminal domain and ring finger 1

Predicted to enable ubiquitin protein ligase activity. Predicted to be located in cytosol. [provided by Alliance of Genome Resources, Mar 2025]

LON peptidase N-terminal domain and ring finger 2 pseudogene

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lon protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lon protease, bacterial/eukaryotic-type protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lon protease homolog, chloroplastic/mitochondrial protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Lon protease homologue 2, peroxisomal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term lon in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase S16, lon N-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Peptidase S16, Lon C-terminal protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From Biocarta Pathways

proteins participating in the thrombin signaling and protease-activated receptors pathway from the Biocarta Pathways dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the serine protease inhibitor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores

proteins localized to the protease inhibitor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the serine protease inhibitor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the protease inhibitor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores

proteins co-occuring with the hsluv protease complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores dataset.

From CTD Gene-Chemical Interactions

genes/proteins interacting with the chemical Protease Inhibitors from the curated CTD Gene-Chemical Interactions dataset.

From GeneRIF Biological Term Annotations

genes co-occuring with the biological term protease in literature-supported statements describing functions of genes from the GeneRIF Biological Term Annotations dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protease location in mast cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the negative regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the positive regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the maintenance of protease location in t cell secretory granule biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Biological Process Annotations 2015

genes participating in the regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the serine protease inhibitor complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Cellular Component Annotations 2015

proteins localized to the protease inhibitor complex cellular component from the curated GO Cellular Component Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the ubiquitin-specific protease binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the sumo-specific protease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the isg15-specific protease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the protease binding molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the nedd8-specific protease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the ubiquitin-specific protease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GO Molecular Function Annotations 2015

genes performing the ubiquitin-like protein-specific protease activity molecular function from the curated GO Molecular Function Annotations 2015 dataset.

From GWAS Catalog SNP-Phenotype Associations

genes associated with the Response to protease inhibitor treatment in hepatitis c (peak serum total bilirubin levels) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Membrane-bound transcription factor site-2 protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protease-activated receptor 4 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protease-activated receptor 2 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protease-activated receptor 3 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Transmembrane protease serine 9 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Apoptotic protease-activating factor 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ubiquitin specific protease, conserved site protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the CAAX amino terminal protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ATP-dependent Clp protease proteolytic subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Retroviral aspartyl protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Mitochondrial inner membrane protease subunit 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Rhomboid serine protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clp protease proteolytic subunit /Translocation-enhancing protein TepA protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Clp protease, ATP-binding subunit ClpX protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Ubiquitin specific protease domain protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protease-activated receptor protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Plasma protease C1 inhibitor protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the CAAX prenyl protease 1 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Tail specific protease protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Gamma-secretase aspartyl protease complex, presenilin enhancer-2 subunit protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the Protease-associated domain, PA protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From InterPro Predicted Protein Domain Annotations

proteins predicted to have the ICP0-binding domain of Ubiquitin-specific protease 7 protein domain from the InterPro Predicted Protein Domain Annotations dataset.

From MPO Gene-Phenotype Associations

gene mutations causing the decreased mast cell protease storage phenotype in transgenic mice from the MPO Gene-Phenotype Associations dataset.

From Phosphosite Textmining Biological Term Annotations

proteins co-occuring with the biological term protease in abstracts of publications describing phosphosites from the Phosphosite Textmining Biological Term Annotations dataset.

From PID Pathways

proteins participating in the Thrombin/protease-activated receptor (PAR) pathway pathway from the PID Pathways dataset.

From DisGeNET Gene-Disease Associations

genes associated with the disease Variably Protease Sensitive Prionopathy in GWAS and other genetic association datasets from the DisGeNET Gene-Disease Associations dataset.

From GO Biological Process Annotations 2023

genes participating in the maintenance of protease location in mast cell secretory granule biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the negative regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the positive regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the protease localization to mast cell secretory granule biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Biological Process Annotations 2023

genes participating in the maintenance of protease location in T cell secretory granule biological process from the curated GO Biological Process Annotations 2023 dataset.

From GO Cellular Component Annotations 2023

proteins localized to the serine protease inhibitor complex cellular component from the curated GO Cellular Component Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the protease binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From GO Molecular Function Annotations 2023

genes performing the ubiquitin-specific protease binding molecular function from the curated GO Molecular Function Annotations 2023 dataset.

From MGI Mouse Phenotype Associations 2023

gene mutations causing the decreased mast cell protease storage phenotype in transgenic mice from the MGI Mouse Phenotype Associations 2023 dataset.

From GO Biological Process Annotations 2025

genes participating in the maintenance of protease location in mast cell secretory granule biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the negative regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the positive regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the regulation of ubiquitin-specific protease activity biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the protease localization to mast cell secretory granule biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Biological Process Annotations 2025

genes participating in the maintenance of protease location in T cell secretory granule biological process from the curated GO Biological Process Annotations 2025 dataset.

From GO Cellular Component Annotations 2025

proteins localized to the serine protease inhibitor complex cellular component from the curated GO Cellular Component Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the protease binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From GO Molecular Function Annotations 2025

genes performing the ubiquitin-specific protease binding molecular function from the curated GO Molecular Function Annotations 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Serine protease inhibitor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Curated Protein Localization Evidence Scores 2025

proteins localized to the Protease inhibitor complex cellular component from the COMPARTMENTS Curated Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the HslUV protease complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Protease inhibitor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025

proteins co-occuring with the Serine protease inhibitor complex cellular component in abstracts of biomedical publications from the COMPARTMENTS Text-mining Protein Localization Evidence Scores 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Plasma factor VII activating protease levels phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Response to protease inhibitor treatment in hepatitis c (bilirubin toxicity) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From GWAS Catalog SNP-Phenotype Associations 2025

genes associated with the Response to protease inhibitor treatment in hepatitis c (peak serum total bilirubin levels) phenotype in GWAS datasets from the GWAS Catalog SNP-Phenotype Associations 2025 dataset.

From DGIdb Drug Targets 2026

interacting proteins for the PROTEASE INHIBITOR drug from theDGIdb Drug Targets 2026 dataset.