close STRING v12.5 is now available!
The next version of STRING is ready for use in your analyses: updated networks across STRING • newly available directed regulatory networks • a new typed view showing functional, physical, and regulatory edges in one network • new clustering options and cluster-based layouts • … and much more!
Explore STRING v12.5 →
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
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ORB31229.1EVE domain-containing protein; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the UPF0310 family. (144 aa)    
Predicted Functional Partners:
ORB31228.1
Pirin; Derived by automated computational analysis using gene prediction method: Protein Homology; Belongs to the pirin family.
       0.781
ORB31227.1
GNAT family N-acetyltransferase; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.780
ORB31226.1
Hypothetical protein; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.686
map
Type I methionyl aminopeptidase; Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed; Belongs to the peptidase M24A family. Methionine aminopeptidase type 1 subfamily.
       0.592
ORB31293.1
Transcriptional regulator; Derived by automated computational analysis using gene prediction method: Protein Homology.
       0.431
Your Current Organism:
Mycolicibacterium parafortuitum
NCBI taxonomy Id: 39692
Other names: ATCC 19686, CCUG 20999, CIP 106802, DSM 43528, JCM 6367, M. parafortuitum, Mycobacterium parafortuitum, NCTC 10411, NRRL B-4035
Server load: low (26%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.