Gene Ontology annotation through association of InterPro records with GO terms

Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity

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

Electronic Gene Ontology annotations created by ARBA machine learning models

Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs

Combined Automated Annotation using Multiple IEA Methods

HtrA2 promotes cell death through its serine protease activity and its ability to antagonize inhibitor of apoptosis proteins.

Critical function of endogenous XIAP in regulating caspase activation during sympathetic neuronal apoptosis.

Integrated analysis of protein composition, tissue diversity, and gene regulation in mouse mitochondria.

Mature DIABLO/Smac is produced by the IMP protease complex on the mitochondrial inner membrane.

MEKK1-induced apoptosis is mediated by Smac/Diablo release from the mitochondria.

Role of Smac/DIABLO in hydrogen peroxide-induced apoptosis in C2C12 myogenic cells.

MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity.

No death without life: vital functions of apoptotic effectors.

Dual specificity phosphatases 18 and 21 target to opposing sides of the mitochondrial inner membrane.

A mitochondrial protein compendium elucidates complex I disease biology.

HOIL-1L interacting protein (HOIP) as an NF-kappaB regulating component of the CD40 signaling complex.

Identification of a novel anti-apoptotic E3 ubiquitin ligase that ubiquitinates antagonists of inhibitor of apoptosis proteins SMAC, HtrA2, and ARTS.

Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins.

Structural and biochemical basis of apoptotic activation by Smac/DIABLO.

Requirement of both the second and third BIR domains for the relief of X-linked inhibitor of apoptosis protein (XIAP)-mediated caspase inhibition by Smac.

The structure of the BIR3 domain of cIAP1 in complex with the N-terminal peptides of SMAC and caspase-9.