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:
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
THUMPD1THUMP domain-containing protein 1; Functions as a tRNA-binding adapter to mediate NAT10- dependent tRNA acetylation (353 aa)    
Predicted Functional Partners:
NAT10
RNA cytidine acetyltransferase; RNA cytidine acetyltransferase with specificity toward both 18S rRNA and tRNAs. Catalyzes the formation of N(4)-acetylcytidine (ac4C) at positions 1337 and 1842 in 18S rRNA (By similarity). Required for early nucleolar cleavages of precursor rRNA at sites A0, A1 and A2 during 18S rRNA synthesis. Catalyzes the formation of ac4C in serine and leucine tRNAs (By similarity). Requires the tRNA-binding adapter protein THUMBD1 for full tRNA acetyltransferase activity but not for 18S rRNA acetylation. Can acetylate both histones and microtubules. Histone acetyla [...]
   
 0.993
CNOT8
CCR4-NOT transcription complex subunit 8; Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. Its function seems to be partially redundant with that of CNOT7. Catalytic component of the CCR4-NOT complex which is linked to various cellular processes including bulk mRNA degradation, miRNA-mediated repression, translational repression during translational initiation and general transcription regulation. During miRNA-mediated repression the complex seems also to act as translational repressor during translational initiation. Additional complex functions may be a [...]
   
  
 0.819
POLE3
DNA polymerase epsilon subunit 3; Forms a complex with DNA polymerase epsilon subunit CHRAC1 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome-remodeling activity of ISWI/SNF2H and ACF1
   
    0.816
PUS7
Pseudouridylate synthase 7
   
 
 0.717
IAPP
Islet amyloid polypeptide; Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism; Belongs to the calcitonin family
      
 0.669
WDR4
tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4; Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. In the complex, it is required to stabilize and induce conformational changes of the catalytic subunit; Belongs to the WD repeat TRM82 family
   
  
 0.652
MB
Myoglobin; Serves as a reserve supply of oxygen and facilitates the movement of oxygen within muscles
      
 0.650
GPN3
GPN-loop GTPase 3; Small GTPase required for proper localization of RNA polymerase II (RNAPII). May act at an RNAP assembly step prior to nuclear import; Belongs to the GPN-loop GTPase family
   
    0.642
TRMT1
tRNA (guanine(26)-N(2))-dimethyltransferase; Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups; Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family
   
 
 0.630
METTL1
tRNA (guanine-N(7)-)-methyltransferase; Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA; Methyltransferase like
   
  
 0.619
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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