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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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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
HSM_2000PFAM: AMP-dependent synthetase and ligase; KEGG: hso:HS_0115 conserved acyl-coenzyme A synthetase-related protein. (426 aa)    
Predicted Functional Partners:
HSM_1998
Putative 3-hydroxymyristoyl/3-hydroxydecanoyl-(acyl-carrier- protein) dehydratase; KEGG: hso:HS_0113 possible 3-hydroxymyristoyl/3-hydroxydecanoyl-[acyl-carrier- protein] dehydratase.
   
 0.992
HSM_2002
PFAM: lipid A biosynthesis acyltransferase; KEGG: hso:HS_0117 possible acyltransferase.
 
     0.947
HSM_1999
Membrane protein-like protein; KEGG: hso:HS_0114 hypothetical protein.
 
     0.946
HSM_2001
PFAM: glycosyl transferase family 2; KEGG: hso:HS_0116 glycosyl transferase, group 2 family protein.
 
 
   0.946
HSM_1997
PFAM: phosphopantetheine-binding; KEGG: hso:HS_0112 acyl carrier protein.
 
 
 0.943
HSM_1996
KEGG: hso:HS_0111 acyl carrier protein.
 
 
 0.939
HSM_2003
KEGG: hso:HS_0118 hypothetical protein.
 
     0.923
HSM_1995
PFAM: phospholipid/glycerol acyltransferase; KEGG: hso:HS_0110 1-acyl-sn-glycerol-3-phosphate acyltransferase.
 
 
 0.901
HSM_1994
KEGG: hso:HS_0109 hypothetical protein.
 
    0.889
HSM_2005
Conserved hypothetical protein; Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane).
 
    0.883
Your Current Organism:
Histophilus somni
NCBI taxonomy Id: 228400
Other names: H. somni 2336, Haemophilus somnus 2336, Histophilus somni 2336, Histophilus somni str. 2336
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