OXR1

OXR1
Identifiers
Aliases	OXR1, TLDC3, Nbla00307, oxidation resistance 1, CHEGDD
External IDs	OMIM: 605609; MGI: 2179326; HomoloGene: 24993; GeneCards: OXR1; OMA:OXR1 - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	106,752,694 bp
Gene location (Mouse)
Chr.	Chromosome 15 (mouse)
End	41,724,444 bp
RNA expression pattern
	Top expressed in
	pons; ; Achilles tendon; ; lateral nuclear group of thalamus; ; trigeminal ganglion; ; sperm; ; spinal ganglia; ; seminal vesicula; ; Brodmann area 23; ; corpus epididymis; ; prefrontal cortex;
	Top expressed in
	medial dorsal nucleus; ; parotid gland; ; subiculum; ; pontine nuclei; ; primary motor cortex; ; habenula; ; medial geniculate nucleus; ; lobe of cerebellum; ; cerebellar vermis; ; inferior colliculi;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; protein binding; molecular function;
Cellular component	nucleolus; mitochondrion; cellular component; nucleoplasm; intracellular membrane-bounded organelle;
Biological process	negative regulation of neuron apoptotic process; response to oxidative stress; cellular response to hydroperoxide; adult walking behavior; neuron apoptotic process; negative regulation of cellular response to oxidative stress; negative regulation of peptidyl-cysteine S-nitrosylation; negative regulation of oxidative stress-induced neuron death;
	Sources:Amigo / QuickGO
Orthologs
	55074
	170719
	ENSG00000164830
	ENSMUSG00000022307
	Q8N573
	Q4KMM3
NM_001198532; NM_001198533; NM_001198534; NM_001198535; NM_018002;
	NM_181354
NM_001130163; NM_001130164; NM_001130165; NM_001130166; NM_130885;
	NM_001358976; NM_001358977; NM_001358978
NP_001185461; NP_001185462; NP_001185463; NP_001185464; NP_060472;
	NP_851999
NP_001123635; NP_001123636; NP_001123637; NP_001123638; NP_570955;
	NP_001345905; NP_001345906; NP_001345907
	Wikidata
View/Edit Human	View/Edit Mouse

Oxidation resistance protein 1 is a protein that in humans is encoded by the OXR1 gene.^[5]^[6] Loss of OXR1 function causes decline of the retromer complex.^[7]