MIF
Gene Ontology Biological Process
- carboxylic acid metabolic process [IDA]
- cell proliferation [IDA]
- cell surface receptor signaling pathway [IDA]
- negative regulation of DNA damage response, signal transduction by p53 class mediator [IDA]
- negative regulation of apoptotic process [IDA]
- negative regulation of cell aging [IDA]
- negative regulation of cell cycle arrest [IDA]
- negative regulation of gene expression [IDA]
- negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator [IDA]
- positive chemotaxis [IDA]
- positive regulation of B cell proliferation [IDA]
- positive regulation of ERK1 and ERK2 cascade [IDA]
- positive regulation of cytokine secretion [IDA]
- positive regulation of fibroblast proliferation [IDA]
- positive regulation of peptidyl-serine phosphorylation [IDA]
- positive regulation of peptidyl-tyrosine phosphorylation [IDA]
- positive regulation of phosphorylation [IDA]
- positive regulation of protein kinase A signaling [IDA]
- prostaglandin biosynthetic process [IDA]
- protein homotrimerization [IPI]
- regulation of macrophage activation [NAS]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
ENO1
Gene Ontology Biological Process
- carbohydrate metabolic process [TAS]
- gluconeogenesis [TAS]
- glucose metabolic process [TAS]
- glycolytic process [TAS]
- negative regulation of cell growth [IDA]
- negative regulation of transcription from RNA polymerase II promoter [TAS]
- negative regulation of transcription, DNA-templated [IDA]
- response to virus [IEP]
- small molecule metabolic process [TAS]
Gene Ontology Molecular Function
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
Exploring an Alternative Cysteine-Reactive Chemistry to Enable Proteome-Wide PPI Analysis by Cross-Linking Mass Spectrometry.
The development of MS-cleavable cross-linking mass spectrometry (XL-MS) has enabled the effective capture and identification of endogenous protein-protein interactions (PPIs) and their residue contacts at the global scale without cell engineering. So far, only lysine-reactive cross-linkers have been successfully applied for proteome-wide PPI profiling. However, lysine cross-linkers alone cannot uncover the complete PPI map in cells. Previously, we have developed ... [more]
Throughput
- High Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| ENO1 MIF | 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 | 0.0824 | BioGRID | 1264657 | |
| ENO1 MIF | 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 | - |
Curated By
- BioGRID