Gene Ontology annotation through association of InterPro records with GO terms

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

Combined Automated Annotation using Multiple IEA Methods

ApoO, a novel apolipoprotein, is an original glycoprotein up-regulated by diabetes in human heart.

Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.

Proteomics analysis of cardiac extracellular matrix remodeling in a porcine model of ischemia/reperfusion injury.

APOOL is a cardiolipin-binding constituent of the Mitofilin/MINOS protein complex determining cristae morphology in mammalian mitochondria.

Apolipoprotein O is mitochondrial and promotes lipotoxicity in heart.

The non-glycosylated isoform of MIC26 is a constituent of the mammalian MICOS complex and promotes formation of crista junctions.

Detailed analysis of the human mitochondrial contact site complex indicate a hierarchy of subunits.

QIL1 is a novel mitochondrial protein required for MICOS complex stability and cristae morphology.

Mass spectrometry analysis of K63-ubiquitinated targets in response to oxidative stress.

Data supporting the role of the non-glycosylated isoform of MIC26 in determining cristae morphology.

Evolution and structural organization of the mitochondrial contact site (MICOS) complex and the mitochondrial intermembrane space bridging (MIB) complex.

Assembly of the Mitochondrial Cristae Organizer Mic10 Is Regulated by Mic26-Mic27 Antagonism and Cardiolipin.

Mutation in the MICOS subunit gene APOO (MIC26) associated with an X-linked recessive mitochondrial myopathy, lactic acidosis, cognitive impairment and autistic features.

MIC26 and MIC27 cooperate to regulate cardiolipin levels and the landscape of OXPHOS complexes.

Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.

Loss of APOO (MIC26) aggravates obesity-related whitening of brown adipose tissue via PPARα-mediated functional interplay between mitochondria and peroxisomes.

MIC26 and MIC27 are bona fide subunits of the MICOS complex in mitochondria and do not exist as glycosylated apolipoproteins.

A X-linked nonsense APOO/MIC26 variant causes a lethal mitochondrial disease with progeria-like phenotypes.

Macrophage-specific deletion of MIC26 (APOO) mitigates advanced atherosclerosis by increasing efferocytosis.

The molecular basis of mitochondrial crista formation by the MIC10 complex.

APOO / MIC26 (Q9BUR5) - N-terminal targeting sequence and paralogue architecture

Affinage mechanistic annotation for APOO (human)

UniProtKB entry Q9BUR5 (MIC26_HUMAN)