BAIT

RING1

RING1A, RNF1, DADB-100D22.6
ring finger protein 1
GO Process (2)
GO Function (1)
GO Component (5)

Gene Ontology Molecular Function

Homo sapiens
PREY

HIST1H2AB

H2A/m, H2AFM
histone cluster 1, H2ab
GO Process (0)
GO Function (1)
GO Component (2)

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

BRCA1/BARD1 site-specific ubiquitylation of nucleosomal H2A is directed by BARD1.

Witus SR, Burrell AL, Farrell DP, Kang J, Wang M, Hansen JM, Pravat A, Tuttle LM, Stewart MD, Brzovic PS, Chatterjee C, Zhao W, DiMaio F, Kollman JM, Klevit RE

Mutations in the E3 ubiquitin ligase RING domains of BRCA1/BARD1 predispose carriers to breast and ovarian cancers. We present the structure of the BRCA1/BARD1 RING heterodimer with the E2 enzyme UbcH5c bound to its cellular target, the nucleosome, along with biochemical data that explain how the complex selectively ubiquitylates lysines 125, 127 and 129 in the flexible C-terminal tail of ... [more]

Nat Struct Mol Biol Dec. 01, 2020; 28(3);268-277 [Pubmed: 33589814]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RING1 HIST1H2AB
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
2906470

Curated By

  • BioGRID