NPM1
Gene Ontology Biological Process
- CENP-A containing nucleosome assembly [TAS]
- DNA repair [IDA]
- cell aging [IMP, ISS]
- centrosome cycle [IMP, ISS]
- intracellular protein transport [TAS]
- negative regulation of apoptotic process [IDA, NAS]
- negative regulation of cell proliferation [IMP, ISS]
- negative regulation of centrosome duplication [IMP]
- negative regulation of protein kinase activity by regulation of protein phosphorylation [IDA]
- nucleocytoplasmic transport [IDA, TAS]
- nucleosome assembly [IDA, TAS]
- positive regulation of NF-kappaB transcription factor activity [IMP]
- positive regulation of translation [IDA]
- protein localization [IDA]
- protein oligomerization [IDA]
- regulation of centriole replication [IMP]
- regulation of eIF2 alpha phosphorylation by dsRNA [IDA]
- regulation of endodeoxyribonuclease activity [IDA]
- regulation of endoribonuclease activity [IDA]
- response to stress [IMP]
- ribosome assembly [TAS]
- signal transduction [NAS]
- viral process [TAS]
Gene Ontology Molecular Function- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
- NF-kappaB binding [IDA, ISS]
- RNA binding [IDA]
- Tat protein binding [IDA]
- histone binding [IDA]
- poly(A) RNA binding [IDA]
- protein binding [IPI]
- protein heterodimerization activity [IMP]
- protein homodimerization activity [IDA]
- protein kinase binding [IPI]
- protein kinase inhibitor activity [IDA]
- ribosomal large subunit binding [IDA]
- ribosomal small subunit binding [IDA]
- transcription coactivator activity [IDA]
- unfolded protein binding [IDA, ISS]
Gene Ontology Cellular Component
TTN
Gene Ontology Biological Process
- blood coagulation [TAS]
- cardiac muscle contraction [IMP]
- cardiac muscle fiber development [IMP]
- cardiac muscle hypertrophy [IMP]
- cardiac muscle tissue morphogenesis [IMP]
- cardiac myofibril assembly [IMP]
- detection of muscle stretch [TAS]
- mitotic chromosome condensation [IEP]
- muscle contraction [NAS, TAS]
- muscle filament sliding [TAS]
- platelet activation [TAS]
- platelet degranulation [TAS]
- regulation of catalytic activity [IMP]
- regulation of protein kinase activity [IMP]
- response to calcium ion [IDA]
- sarcomere organization [IMP]
- sarcomerogenesis [IMP]
- skeletal muscle myosin thick filament assembly [IMP]
- skeletal muscle thin filament assembly [IMP]
- striated muscle contraction [TAS]
Gene Ontology Molecular Function- actin filament binding [IDA]
- actinin binding [IDA, IPI]
- calcium ion binding [IDA]
- calmodulin binding [IPI, TAS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- muscle alpha-actinin binding [IPI]
- protease binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein self-association [IDA]
- protein serine/threonine kinase activity [IDA]
- structural constituent of muscle [IMP, TAS]
- structural molecule activity conferring elasticity [TAS]
- telethonin binding [IPI, ISS]
- actin filament binding [IDA]
- actinin binding [IDA, IPI]
- calcium ion binding [IDA]
- calmodulin binding [IPI, TAS]
- enzyme binding [IPI]
- identical protein binding [IPI]
- muscle alpha-actinin binding [IPI]
- protease binding [IPI]
- protein binding [IPI]
- protein kinase binding [IPI]
- protein self-association [IDA]
- protein serine/threonine kinase activity [IDA]
- structural constituent of muscle [IMP, TAS]
- structural molecule activity conferring elasticity [TAS]
- telethonin binding [IPI, ISS]
Gene Ontology Cellular Component
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).
Publication
In-Depth In Vivo Crosslinking in Minutes by a Compact, Membrane-Permeable, and Alkynyl-Enrichable Crosslinker.
Chemical crosslinking coupled with mass spectrometry (CXMS) has emerged as a powerful technique to obtain the dynamic conformations and interaction interfaces of protein complexes. Limited by the poor cell membrane permeability, chemical reactivity, and biocompatibility of crosslinkers, in vivo crosslinking to capture the dynamics of protein complexes with finer temporal resolution and higher coverage is attractive but challenging. In this ... [more]
Throughput
- High Throughput
Additional Notes
- High confidence crosslinked peptides were identified with the FDR set to 0.01 at the peptide-spectrum matches (PSM) level and PSMs >= 2.
- MS non-cleavable crosslinker of bis(succinimidyl) with propargyl tag (BSP)
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| NPM1 TTN | 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 | - | |
| NPM1 TTN | Proximity Label-MS Proximity Label-MS An interaction is inferred when a bait-enzyme fusion protein selectively modifies a vicinal protein with a diffusible reactive product, followed by affinity capture of the modified protein and identification by mass spectrometric methods. | High | - | BioGRID | 2784634 |
Curated By
- BioGRID