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
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Score
dot1Histone-lysine N-methyltransferase, H3 lysine-79 specific; Histone methyltransferase that specifically trimethylates histone H3 to form H3K79me3. This methylation is required for telomere silencing and for the pachytene checkpoint during the meiotic cell cycle by allowing the recruitment of RAD9 to double strand breaks. Nucleosomes are preferred as substrate compared to free histone. (501 aa)    
Predicted Functional Partners:
set1
Histone-lysine N-methyltransferase, H3 lysine-4 specific; Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation. Belongs to the class V-like SAM-binding methyltransferase superfamily.
   
 0.986
set2
Histone-lysine N-methyltransferase, H3 lysine-36 specific; Histone methyltransferase that trimethylates histone H3 'Lys- 36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression; Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. SET2 subfamily.
   
 0.977
hhtA
Histone H3; 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.
   
 0.969
set9
Histone-lysine N-methyltransferase set9; Histone methyltransferase that trimethylates 'Lys-20' of histone H4 to form H4K20me3.
   
 
 0.962
ANIA_04764
Histone-lysine N-methyltransferase (Ash1), putative (AFU_orthologue AFUA_3G06480).
    
 0.938
ANIA_06554
Histone domain-containing protein.
   
 0.934
ANIA_05998
SET and MYND domain protein, putative (AFU_orthologue AFUA_2G10080).
    
 0.923
ANIA_10501
annotation not available
    
   0.865
htaA
Histone H2A; Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. 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.
    
 
 0.861
hhfA
Histone H4.1; 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.
   
 
 0.844
Your Current Organism:
Aspergillus nidulans
NCBI taxonomy Id: 227321
Other names: A. nidulans FGSC A4, Aspergillus nidulans FGSC A4, Emericella nidulans FGSC A4
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.