MEP1A
Gene Ontology Cellular Component
CALR
Gene Ontology Biological Process
- cell cycle arrest [ISO]
- cellular senescence [IMP, ISO]
- chaperone-mediated protein folding [ISO]
- cortical actin cytoskeleton organization [IDA]
- negative regulation of intracellular steroid hormone receptor signaling pathway [ISO]
- negative regulation of neuron differentiation [ISO]
- negative regulation of retinoic acid receptor signaling pathway [ISO]
- negative regulation of transcription from RNA polymerase II promoter [ISO]
- negative regulation of transcription, DNA-templated [ISO]
- negative regulation of translation [ISO]
- peptide antigen assembly with MHC class I protein complex [IMP]
- positive regulation of DNA replication [ISO]
- positive regulation of cell cycle [IMP, ISO]
- positive regulation of cell proliferation [ISO]
- positive regulation of dendritic cell chemotaxis [ISO]
- positive regulation of gene expression [IMP]
- positive regulation of phagocytosis [IMP]
- positive regulation of substrate adhesion-dependent cell spreading [ISO]
- protein export from nucleus [ISO]
- protein localization to nucleus [IMP, ISO]
- protein stabilization [IDA]
- regulation of meiosis [IDA]
Gene Ontology Molecular Function- androgen receptor binding [ISO]
- calcium ion binding [IDA, ISO]
- carbohydrate binding [IDA]
- glycoprotein binding [ISO]
- hormone binding [ISO]
- integrin binding [ISO]
- iron ion binding [ISO]
- mRNA binding [IDA, ISO]
- peptide binding [ISO]
- poly(A) RNA binding [ISO]
- protein binding [IPI]
- ubiquitin protein ligase binding [ISO]
- unfolded protein binding [ISO]
- androgen receptor binding [ISO]
- calcium ion binding [IDA, ISO]
- carbohydrate binding [IDA]
- glycoprotein binding [ISO]
- hormone binding [ISO]
- integrin binding [ISO]
- iron ion binding [ISO]
- mRNA binding [IDA, ISO]
- peptide binding [ISO]
- poly(A) RNA binding [ISO]
- protein binding [IPI]
- ubiquitin protein ligase binding [ISO]
- unfolded protein binding [ISO]
Gene Ontology Cellular Component
- Golgi apparatus [ISO]
- MHC class I peptide loading complex [IMP]
- acrosomal vesicle [ISO]
- cell surface [ISO]
- cytoplasm [ISO]
- cytosol [ISO]
- endoplasmic reticulum [IDA, ISO, ISS]
- endoplasmic reticulum lumen [IDA, ISO]
- external side of plasma membrane [IDA]
- extracellular matrix [ISO]
- extracellular space [IDA, ISO]
- extracellular vesicular exosome [ISO]
- focal adhesion [ISO]
- intracellular membrane-bounded organelle [ISO]
- membrane [ISO]
- nucleus [ISO]
- perinuclear region of cytoplasm [ISO]
- polysome [IDA]
- protein complex [ISO]
- sarcoplasmic reticulum [ISO]
- smooth endoplasmic reticulum [ISO]
Affinity Capture-Western
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.
Publication
Chaperone interactions of the metalloproteinase meprin A in the secretory or proteasomal-degradative pathway.
The secreted form of mouse meprin A is a homooligomer of meprin alpha subunits that contain a prosequence, a catalytic domain, and three domains designated as MAM (meprin, A5 protein, receptor protein-tyrosine phosphatase mu), MATH (meprin and TRAF homology), and AM (AfterMath). Previous studies indicated that wild-type mouse meprin alpha is predominantly a secreted protein, while the MAM deletion mutant ... [more]
Throughput
- Low Throughput
Curated By
- BioGRID