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Bra001445 protein (Brassica rapa) - STRING interaction network
"Bra001445" - AT3G12270 in Brassica rapa
Nodes:
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splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
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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:
some 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 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
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
Bra001445AT3G12270 (E=3e-136) ATPRMT3, PRMT3 | PRMT3 (PROTEIN ARGININE METHYLTRANSFERASE 3); methyltransferase/ zinc ion binding (299 aa)    
Predicted Functional Partners:
Bra028311
AT5G52470 (E=2e-025) FIB1, FBR1, ATFIB1, ATFBR1, SKIP7 | FIB1 (FIBRILLARIN 1); snoRNA binding (189 aa)
     
 
  0.926
Bra022595
AT4G25630 (E=4e-118) FIB2, ATFIB2 | FIB2 (FIBRILLARIN 2); snoRNA binding (291 aa)
     
 
  0.926
Bra019148
AT4G25630 (E=3e-129) FIB2, ATFIB2 | FIB2 (FIBRILLARIN 2); snoRNA binding (307 aa)
     
 
  0.926
Bra013905
AT4G25630 (E=4e-127) FIB2, ATFIB2 | FIB2 (FIBRILLARIN 2); snoRNA binding (310 aa)
     
 
  0.926
Bra010455
AT4G25630 (E=1e-114) FIB2, ATFIB2 | FIB2 (FIBRILLARIN 2); snoRNA binding (291 aa)
     
 
  0.926
Bra011929
AT5G59690 (E=2e-040) | histone H4 ; 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 (103 aa)
       
  0.858
Bra000481
AT5G59690 (E=3e-041) | histone H4 ; 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 (103 aa)
       
  0.858
Bra031594.1-P
AT5G59690 (E=3e-041) | histone H4 (103 aa)
       
  0.858
Bra030704
AT5G59690 (E=4e-039) | histone H4 ; 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 (103 aa)
       
  0.858
Bra020297
AT5G59690 (E=9e-041) | histone H4 ; 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 (103 aa)
       
  0.858
Your Current Organism:
Brassica rapa
NCBI taxonomy Id: 3711
Other names: B. rapa, Brassica, Brassica L., Brassica rapa, Brassica rapa L., Brassiceae, field mustard
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