STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
RNF20E3 ubiquitin-protein ligase BRE1A; Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). (1028 aa)    
Predicted Functional Partners:
UBE2B
Ubiquitin conjugating enzyme E2 B; Belongs to the ubiquitin-conjugating enzyme family.
    
 0.981
UBE2A
Ubiquitin-conjugating enzyme; Belongs to the ubiquitin-conjugating enzyme family.
    
 0.965
SETD2
SET domain containing 2, histone lysine methyltransferase.
   
 
 0.827
LOC107053803
Histone H2B 7; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
    
 
 0.808
HIST1H2B8
Histone H2B 8; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
    
 
 0.808
H2BE1
Histone H2B; Belongs to the histone H2B family.
    
 
 0.808
HIST1H2B5L
Histone H2B; Belongs to the histone H2B family.
    
 
 0.808
HIST1H2B5
Histone H2B 5; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
    
 
 0.808
HIST1H2BO
Histone H2B 1/2/3/4/6; Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
    
 
 0.792
USP22
Ubiquitin carboxyl-terminal hydrolase.
    
 
 0.778
Your Current Organism:
Gallus gallus
NCBI taxonomy Id: 9031
Other names: G. gallus, Gallus domesticus, Gallus gallus domesticus, bantam, chicken, chickens, dwarf Leghorn chickens, red junglefowl
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.