BAIT
ACTB
BRWS1, PS1TP5BP1
actin, beta
GO Process (17)
GO Function (8)
GO Component (15)
Gene Ontology Biological Process
- 'de novo' posttranslational protein folding [TAS]
- ATP-dependent chromatin remodeling [IDA]
- Fc-gamma receptor signaling pathway involved in phagocytosis [TAS]
- adherens junction organization [TAS]
- axon guidance [TAS]
- blood coagulation [TAS]
- cell junction assembly [TAS]
- cell-cell junction organization [TAS]
- cellular component movement [TAS]
- cellular protein metabolic process [TAS]
- chromatin organization [TAS]
- innate immune response [TAS]
- membrane organization [TAS]
- platelet aggregation [IMP]
- protein folding [TAS]
- retina homeostasis [IEP]
- substantia nigra development [IEP]
Gene Ontology Molecular Function- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- Tat protein binding [IPI]
- kinesin binding [IPI]
- nitric-oxide synthase binding [IPI]
- nucleosomal DNA binding [IDA]
- protein binding [IPI]
- structural constituent of cytoskeleton [TAS]
- RNA polymerase II core promoter proximal region sequence-specific DNA binding [IDA]
- RNA polymerase II distal enhancer sequence-specific DNA binding [IDA]
- Tat protein binding [IPI]
- kinesin binding [IPI]
- nitric-oxide synthase binding [IPI]
- nucleosomal DNA binding [IDA]
- protein binding [IPI]
- structural constituent of cytoskeleton [TAS]
Gene Ontology Cellular Component
- MLL5-L complex [IDA]
- NuA4 histone acetyltransferase complex [IDA]
- blood microparticle [IDA]
- cytoplasm [TAS]
- cytoplasmic ribonucleoprotein granule [IDA]
- cytoskeleton [TAS]
- cytosol [TAS]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- membrane [IDA]
- nuclear chromatin [IDA]
- nucleoplasm [TAS]
- protein complex [IDA]
- ribonucleoprotein complex [IDA]
Homo sapiens
PREY
PCYT1B
CCTB, CTB
phosphate cytidylyltransferase 1, choline, beta
GO Process (5)
GO Function (0)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Cellular Component
Homo sapiens
Co-crystal Structure
Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.
Publication
Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT.
The 30-A cryo-EM-derived structure of apo-CCT-alpha-actin shows actin opened up across its nucleotide-binding cleft and binding to either of two CCT subunit pairs, CCTbeta-CCTdelta or CCTepsilon-CCTdelta, in a similar 1:4 arrangement. The two main duplicated domains of native actin are linked twice, topologically, by the connecting residues, Q137-S145 and P333-S338, and are tightly held together by hydrogen bonding with bound ... [more]
J. Struct. Biol. Aug. 01, 2001; 135(2);198-204 [Pubmed: 11580269]
Throughput
- Low Throughput
Curated By
- BioGRID