BAIT

RL2

HHV1gp082
contains a RING finger; disrupts ND10; proteasome-dependent degradation of several cellular proteins
GO Process (0)
GO Function (0)
GO Component (0)
Human Herpesvirus 1
PREY

UBE2D1

E2(17)KB1, SFT, UBC4/5, UBCH5, UBCH5A
ubiquitin-conjugating enzyme E2D 1
GO Process (24)
GO Function (3)
GO Component (5)
Homo sapiens

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Herpes simplex virus type 1 immediate-early protein ICP0 and is isolated RING finger domain act as ubiquitin E3 ligases in vitro.

Boutell C, Sadis S, Everett RD

Proteasome-dependent degradation of ubiquitinated proteins plays a key role in many important cellular processes. Ubiquitination requires the E1 ubiquitin activating enzyme, an E2 ubiquitin conjugating enzyme, and frequently a substrate-specific ubiquitin protein ligase (E3). One class of E3 ubiquitin ligases has been shown to contain a common zinc-binding RING finger motif. We have previously shown that herpes simplex virus type ... [more]

J. Virol. Jan. 01, 2002; 76(2);841-50 [Pubmed: 11752173]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
UBE2D1 RL2
Two-hybrid
Two-hybrid

Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation.

Low-BioGRID
-

Curated By

  • BioGRID