PREY

MEF2A

ADCAD1, RSRFC4, RSRFC9, mef2
myocyte enhancer factor 2A
GO Process (31)
GO Function (15)
GO Component (5)
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

A molecular basis for phosphorylation-dependent SUMO conjugation by the E2 UBC9.

Mohideen F, Capili AD, Bilimoria PM, Yamada T, Bonni A, Lima CD

Phosphorylation and small ubiquitin-like modifier (SUMO) conjugation contribute to the spatial and temporal regulation of substrates containing phosphorylation-dependent SUMO consensus motifs (PDSMs). Myocyte-enhancement factor 2 (MEF2) is a transcription factor and PDSM substrate whose modification by SUMO drives postsynaptic dendritic differentiation. NMR analysis revealed that the human SUMO E2 interacted with model substrates for phosphorylated and nonphosphorylated MEF2 in similar ... [more]

Nat. Struct. Mol. Biol. Sep. 01, 2009; 16(9);945-52 [Pubmed: 19684601]

Throughput

  • Low Throughput

Additional Notes

  • NMR

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBE2I MEF2A
Biochemical Activity
Biochemical Activity

An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.

Low-BioGRID
679342

Curated By

  • BioGRID