BAIT
RNF167
5730408C10Rik, RING105, LP2254
ring finger protein 167
GO Process (2)
GO Function (2)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Homo sapiens
PREY
ATP2A1
ATP2A, SERCA1
ATPase, Ca++ transporting, cardiac muscle, fast twitch 1
GO Process (18)
GO Function (5)
GO Component (11)
Gene Ontology Biological Process
- ATP catabolic process [ISS]
- apoptotic mitochondrial changes [IMP]
- blood coagulation [TAS]
- calcium ion import [IMP]
- calcium ion transmembrane transport [IDA]
- calcium ion transport [IDA, IMP]
- intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [IMP]
- ion transmembrane transport [TAS]
- maintenance of mitochondrion location [IMP]
- negative regulation of endoplasmic reticulum calcium ion concentration [IMP]
- negative regulation of striated muscle contraction [IMP]
- positive regulation of endoplasmic reticulum calcium ion concentration [IMP]
- positive regulation of fast-twitch skeletal muscle fiber contraction [IDA]
- positive regulation of mitochondrial calcium ion concentration [IMP]
- regulation of striated muscle contraction [IMP]
- relaxation of skeletal muscle [IDA]
- response to endoplasmic reticulum stress [IMP]
- transmembrane transport [TAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
- H zone [IDA]
- I band [IDA]
- calcium channel complex [IC]
- endoplasmic reticulum membrane [IDA, TAS]
- endoplasmic reticulum-Golgi intermediate compartment [ISS]
- integral component of membrane [NAS]
- membrane [ISS]
- perinuclear region of cytoplasm [ISS]
- platelet dense tubular network membrane [TAS]
- sarcoplasmic reticulum [ISS, NAS]
- sarcoplasmic reticulum membrane [IC, TAS]
Homo sapiens
Two-hybrid
Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.
Publication
A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome.
The complexity of the skeletal muscle and the identification of numerous human disease-causing mutations in its constitutive proteins make it an interesting tissue for proteomic studies aimed at understanding functional relationships of interacting proteins in both health and diseases.We undertook a large-scale study using two-hybrid screens and a human skeletal-muscle cDNA library to establish a proteome-scale map of protein-protein interactions ... [more]
Skelet Muscle Feb. 19, 2013; 3(1);3 [Pubmed: 23414517]
Throughput
- High Throughput
Curated By
- BioGRID