BAIT
PRMT8
HRMT1L3, HRMT1L4
protein arginine methyltransferase 8
GO Process (7)
GO Function (9)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IBA]
- histone-arginine N-methyltransferase activity [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA]
- protein-arginine omega-N asymmetric methyltransferase activity [IDA]
- protein-arginine omega-N monomethyltransferase activity [IDA]
- S-adenosylmethionine-dependent methyltransferase activity [IDA]
- histone methyltransferase activity (H4-R3 specific) [IBA]
- histone-arginine N-methyltransferase activity [IDA]
- identical protein binding [IPI]
- protein binding [IPI]
- protein heterodimerization activity [IDA]
- protein homodimerization activity [IDA]
- protein-arginine omega-N asymmetric methyltransferase activity [IDA]
- protein-arginine omega-N monomethyltransferase activity [IDA]
Homo sapiens
PREY
HSPA1B
HSP70-1B, HSP70-2, DAAP-21F2.7
heat shock 70kDa protein 1B
GO Process (20)
GO Function (13)
GO Component (17)
Gene Ontology Biological Process
- ATP catabolic process [IDA]
- RNA metabolic process [TAS]
- cellular heat acclimation [IMP]
- cellular response to heat [IDA]
- cellular response to oxidative stress [TAS]
- gene expression [TAS]
- mRNA catabolic process [IDA]
- mRNA metabolic process [TAS]
- negative regulation of apoptotic process [IMP, TAS]
- negative regulation of cell death [IDA, IMP]
- negative regulation of cell growth [IMP]
- negative regulation of cell proliferation [IMP]
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand [IMP]
- negative regulation of inclusion body assembly [IDA]
- negative regulation of protein ubiquitination [IDA]
- positive regulation of erythrocyte differentiation [IMP]
- protein refolding [IDA]
- protein stabilization [TAS]
- regulation of cell death [IMP]
- response to unfolded protein [IDA]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
- ATP binding [IDA]
- ATPase activity [IDA]
- ATPase activity, coupled [IDA]
- G-protein coupled receptor binding [IPI]
- double-stranded RNA binding [IDA]
- enzyme binding [IPI]
- heat shock protein binding [IPI]
- poly(A) RNA binding [IDA]
- protein N-terminus binding [IPI]
- protein binding [IPI]
- protein binding involved in protein folding [IDA]
- ubiquitin protein ligase binding [IPI]
- unfolded protein binding [IDA, NAS, TAS]
Gene Ontology Cellular Component
- COP9 signalosome [IDA]
- aggresome [IDA]
- blood microparticle [IDA]
- centriole [IDA]
- cytoplasm [IDA, TAS]
- cytosol [IDA, TAS]
- endoplasmic reticulum [TAS]
- extracellular vesicular exosome [IDA]
- focal adhesion [IDA]
- inclusion body [IDA]
- mitochondrion [TAS]
- nuclear speck [IDA]
- nucleus [IDA]
- perinuclear region of cytoplasm [IDA]
- ribonucleoprotein complex [IDA]
- ubiquitin ligase complex [IDA]
- vesicle [IDA]
Homo sapiens
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
Identification of proteins interacting with protein arginine methyltransferase 8: the Ewing sarcoma (EWS) protein binds independent of its methylation state.
Protein arginine methylation is a eukaryotic posttranslational modification that plays a role in transcription, mRNA splicing and transport, in protein-protein interaction, and cell signaling. The type I protein arginine methyltransferase (PRMT) 8 is the only member of the human PRMT family that is localized at the cell membrane and its endogenous substrates have remained unknown as yet. Although PRMT8 was ... [more]
Proteins Sep. 01, 2008; 72(4);1125-37 [Pubmed: 18320585]
Throughput
- Low Throughput
Curated By
- BioGRID