CCAR2
Gene Ontology Biological Process
- RNA splicing [IMP]
- mitochondrial fragmentation involved in apoptotic process [IDA]
- negative regulation of catalytic activity [IDA, IMP]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage [IMP]
- negative regulation of proteasomal ubiquitin-dependent protein catabolic process [IDA]
- positive regulation of DNA damage checkpoint [IMP]
- positive regulation of apoptotic process [IMP]
- regulation of DNA-templated transcription, elongation [IMP]
- regulation of circadian rhythm [ISS]
- regulation of protein stability [IDA]
- response to UV [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
HSPD1
Gene Ontology Biological Process
- 'de novo' protein folding [ISS]
- ATP catabolic process [ISS]
- B cell activation [IDA]
- B cell cytokine production [IDA]
- B cell proliferation [IDA]
- MyD88-dependent toll-like receptor signaling pathway [IDA]
- T cell activation [IDA]
- activation of cysteine-type endopeptidase activity involved in apoptotic process [IDA]
- chaperone-mediated protein complex assembly [ISS]
- isotype switching to IgG isotypes [IDA]
- negative regulation of apoptotic process [IMP]
- positive regulation of T cell activation [IDA, ISS]
- positive regulation of T cell mediated immune response to tumor cell [IDA]
- positive regulation of apoptotic process [IMP]
- positive regulation of interferon-alpha production [IDA]
- positive regulation of interferon-gamma production [IDA, ISS]
- positive regulation of interleukin-10 production [IDA]
- positive regulation of interleukin-12 production [IDA]
- positive regulation of interleukin-6 production [IDA]
- positive regulation of macrophage activation [IDA]
- protein maturation [ISS]
- protein refolding [IDA]
- protein stabilization [IMP, ISS]
- response to unfolded protein [IDA]
Gene Ontology Molecular Function- ATPase activity [ISS]
- DNA replication origin binding [ISS]
- chaperone binding [IPI]
- double-stranded RNA binding [IDA]
- lipopolysaccharide binding [IDA]
- p53 binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [ISS]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IC, ISS]
- ATPase activity [ISS]
- DNA replication origin binding [ISS]
- chaperone binding [IPI]
- double-stranded RNA binding [IDA]
- lipopolysaccharide binding [IDA]
- p53 binding [IPI]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- single-stranded DNA binding [ISS]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IC, ISS]
Gene Ontology Cellular Component
- cell surface [IDA]
- coated pit [IDA]
- coated vesicle [IDA]
- cyclin-dependent protein kinase activating kinase holoenzyme complex [IDA]
- cytoplasm [IDA]
- cytosol [IDA]
- early endosome [IDA]
- extracellular space [IDA]
- extracellular vesicular exosome [IDA]
- lipopolysaccharide receptor complex [IDA]
- membrane [IDA]
- mitochondrial inner membrane [ISS]
- mitochondrial matrix [TAS]
- mitochondrion [IDA]
- protein complex [IDA]
- secretory granule [ISS]
Affinity Capture-MS
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 is identified by mass spectrometric methods.
Publication
DBC1, p300, HDAC3, and Siah1 coordinately regulate ELL stability and function for expression of its target genes.
Among all of the Super Elongation Complex (SEC) components, ELL1 (also known as ELL) is the only bona fide elongation factor that directly stimulates transcription elongation by RNA polymerase II. However, the mechanism(s) of functional regulation of ELL1 (referred to as ELL hereafter), through its stabilization, is completely unknown. Here, we report a function of human DBC1 in regulating ELL ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| HSPD1 CCAR2 | Co-fractionation Co-fractionation Interaction inferred from the presence of two or more protein subunits in a partially purified protein preparation. If co-fractionation is demonstrated between 3 or more proteins, then add them as a complex. | High | 1 | BioGRID | 1259662 | |
| CCAR2 HSPD1 | Cross-Linking-MS (XL-MS) Cross-Linking-MS (XL-MS) An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071). | High | - | BioGRID | 3676060 |
Curated By
- BioGRID