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

Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara

Electronic Gene Ontology annotations created by ARBA machine learning models

Combined Automated Annotation using Multiple IEA Methods

The protease core of the muscle-specific calpain, p94, undergoes Ca2+-dependent intramolecular autolysis.

NF-kappaB-dependent expression of the antiapoptotic factor c-FLIP is regulated by calpain 3, the protein involved in limb-girdle muscular dystrophy type 2A.

Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle.

Novel variants of muscle calpain 3 identified in human melanoma cells: cisplatin-induced changes in vitro and differential expression in melanocytic lesions.

Immunohistochemical analysis of calpain 3: advantages and limitations in diagnosing LGMD2A.

Calpain 3 is a rapid-action, unidirectional proteolytic switch central to muscle remodeling.

A new pathway encompassing calpain 3 and its newly identified substrate cardiac ankyrin repeat protein is involved in the regulation of the nuclear factor-κB pathway in skeletal muscle.

Def defines a conserved nucleolar pathway that leads p53 to proteasome-independent degradation.

A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome.

PLEIAD/SIMC1/C5orf25, a novel autolysis regulator for a skeletal-muscle-specific calpain, CAPN3, scaffolds a CAPN3 substrate, CTBP1.

A proteome-scale map of the human interactome network.

Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types. Specific expression of the mRNA in skeletal muscle.

Widespread Expansion of Protein Interaction Capabilities by Alternative Splicing.

Phosphorylation of Def Regulates Nucleolar p53 Turnover and Cell Cycle Progression through Def Recruitment of Calpain3.

Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.

Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A.

Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A.

Skeletal muscle-specific calpain is an intracellular Na+-dependent protease.

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy.

Non-proteolytic functions of calpain-3 in sarcoplasmic reticulum in skeletal muscles.

Calpain-3 Is Not a Sodium Dependent Protease and Simply Requires Calcium for Activation.

Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin.

Withdrawal: Human calpain-3 and its structural plasticity: Dissociation of a homohexamer into dimers on binding titin.

Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle.

Down-regulation of MyoD by calpain 3 promotes generation of reserve cells in C2C12 myoblasts.