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  • 11.0 [archived version]
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DLEU7 DLEU7 ARL14EPL ARL14EPL ENSG00000268714 ENSG00000268714 BAZ2A BAZ2A ATF7IP ATF7IP SETDB2 SETDB2 ARL14EP ARL14EP PLOD2 PLOD2 PLOD3 PLOD3 CAMKMT CAMKMT PHF11 PHF11
"SETDB2" - Histone-lysine N-methyltransferase SETDB2 in Homo sapiens
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
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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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SETDB2Histone-lysine N-methyltransferase SETDB2; Histone methyltransferase involved in left-right axis specification in early development and mitosis. Specifically trimethylates ’Lys-9’ of histone H3 (H3K9me3). H3K9me3 is a specific tag for epigenetic transcriptional repression that recruits HP1 (CBX1, CBX3 and/or CBX5) proteins to methylated histones. Contributes to H3K9me3 in both the interspersed repetitive elements and centromere-associated repeats. Plays a role in chromosome condensation and segregation during mitosis; Lysine methyltransferases (719 aa)    
Predicted Functional Partners:
PHF11
PHD finger protein 11; Positive regulator of Th1-type cytokine gene expression; PHD finger proteins (331 aa)
 
 
   
  0.912
ARL14EP
ARL14 effector protein; Through its interaction with ARL14 and MYO1E, may connect MHC class II-containing cytoplasmic vesicles to the actin network and hence controls the movement of these vesicles along the actin cytoskeleton in dendritic cells (260 aa)
       
      0.831
ATF7IP
Activating transcription factor 7-interacting protein 1; Recruiter that couples transcriptional factors to general transcription apparatus and thereby modulates transcription regulation and chromatin formation. Can both act as an activator or a repressor depending on the context. Mediates MBD1-dependent transcriptional repression, probably by recruiting complexes containing SETDB1. Required to stimulate histone methyltransferase activity of SETDB1 and facilitate the conversion of dimethylated to trimethylated H3 ’Lys-9’ (H3K9me3). The complex formed with MBD1 and SETDB1 represses trans [...] (1278 aa)
     
 
  0.770
CAMKMT
Calmodulin-lysine N-methyltransferase; Catalyzes the trimethylation of ’Lys-116’ in calmodulin; Seven-beta-strand methyltransferase motif containing (323 aa)
         
  0.725
BAZ2A
Bromodomain adjacent to zinc finger domain protein 2A; Essential component of the NoRC (nucleolar remodeling complex) complex, a complex that mediates silencing of a fraction of rDNA by recruiting histone-modifying enzymes and DNA methyltransferases, leading to heterochromatin formation and transcriptional silencing. In the complex, it plays a central role by being recruited to rDNA and by targeting chromatin modifying enzymes such as HDAC1, leading to repress RNA polymerase I transcription. Recruited to rDNA via its interaction with TTF1 and its ability to recognize and bind histone H [...] (1905 aa)
     
 
  0.713
ARL14EPL
ARL14 effector protein-like; ADP ribosylation factor like GTPase 14 effector protein like (152 aa)
       
      0.661
ENSG00000268714
annotation not available (81 aa)
       
      0.661
DLEU7
Leukemia-associated protein 7; Deleted in lymphocytic leukemia, 7 (160 aa)
           
  0.653
PLOD2
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (758 aa)
     
 
    0.651
PLOD3
Procollagen-lysine,2-oxoglutarate 5-dioxygenase 3; Forms hydroxylysine residues in -Xaa-Lys-Gly- sequences in collagens. These hydroxylysines serve as sites of attachment for carbohydrate units and are essential for the stability of the intermolecular collagen cross-links (738 aa)
     
 
    0.651
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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