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.
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query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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naa40N-alpha-acetyltransferase 40; N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A. In contrast to other N-alpha-acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg-Gly sequence'. Belongs to the acetyltransferase family. NAA40 subfamily. (237 aa)    
Predicted Functional Partners:
naa20
N-alpha-acetyltransferase 20; Catalytic subunit of the NatB complex which catalyzes acetylation of the N-terminal methionine residues of peptides beginning with Met-Asp, Met-Glu, Met-Asn and Met-Gln. Proteins with cell cycle functions are overrepresented in the pool of NatB substrates. Required for maintaining the structure and function of actomyosin fibers and for proper cellular migration.
      
 0.988
naa50
N-alpha-acetyltransferase 50; N-alpha-acetyltransferase that acetylates the N-terminus of proteins that retain their initiating methionine (By similarity). Has a broad substrate specificity: able to acetylate the initiator methionine of most peptides, except for those with a proline in second position (By similarity). Also displays N-epsilon-acetyltransferase activity by mediating acetylation of the side chain of specific lysines on proteins (By similarity). The relevance of N-epsilon-acetyltransferase activity is however unclear (By similarity). Required for sister chromatid cohesion [...]
   
  
 0.972
naa30
N(alpha)-acetyltransferase 30, NatC catalytic subunit.
      
 0.958
nat15
N-alpha-acetyltransferase 60; N-alpha-acetyltransferase that specifically mediates the acetylation of N-terminal residues of the transmembrane proteins, with a strong preference for N-termini facing the cytosol. Displays N- terminal acetyltransferase activity towards a range of N-terminal sequences including those starting with Met-Lys, Met-Val, Met-Ala and Met-Met. Required for normal chromosomal segregation during anaphase. May also show histone acetyltransferase activity; such results are however unclear in vivo and would require additional experimental evidences.
      
 0.956
wdr11
WD repeat-containing protein 11; Involved in the Hedgehog (Hh) signaling pathway, is essential for normal ciliogenesis. Regulates the proteolytic processing of gli3 and cooperates with the transcription factor emx1 in the induction of downstream Hh pathway gene expression and gonadotropin-releasing hormone production. WDR11 complex facilitates the tethering of Adaptor protein-1 complex (AP-1)-derived vesicles.
    
   0.890
xpot
Exportin-T; Mediates the nuclear export of aminoacylated tRNAs. Belongs to the exportin family.
    
   0.888
naa25
N(alpha)-acetyltransferase 25, NatB auxiliary subunit.
      
 0.854
naa80
N(alpha)-acetyltransferase 80, NatH catalytic subunit.
      
 0.809
naa10
N(alpha)-acetyltransferase 10, NatA catalytic subunit.
   
  
 0.772
pop7
Ribonuclease P protein subunit p20; Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences.
      
 0.739
Your Current Organism:
Danio rerio
NCBI taxonomy Id: 7955
Other names: Brachydanio rerio, Brachydanio rerio frankei, Cyprinus rerio, D. rerio, Danio frankei, Danio rerio frankei, leopard danio, zebra danio, zebra fish, zebrafish
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