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STRINGSTRING
MICU3 MICU3 RPUSD1 RPUSD1 RPUSD2 RPUSD2 SETD5 SETD5 RPUSD3 RPUSD3 QTRTD1 QTRTD1 THUMPD3 THUMPD3 VPS35 VPS35 TRMT11 TRMT11 TRMT112 TRMT112 ZMYM3 ZMYM3
"THUMPD3" - THUMP domain-containing protein 3 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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THUMPD3THUMP domain-containing protein 3; Seven-beta-strand methyltransferase motif containing; Belongs to the methyltransferase superfamily (507 aa)    
Predicted Functional Partners:
SETD5
SET domain-containing protein 5; Probable transcriptional regulator that acts via the formation of large multiprotein complexes that modify and/or remodel the chromatin. Acts as a regulator of histone acetylation during gene transcription; SET domain containing (1442 aa)
            
  0.813
MICU3
Calcium uptake protein 3, mitochondrial; May play a role in mitochondrial calcium uptake; EF-hand domain containing (530 aa)
        
      0.808
VPS35
Vacuolar protein sorting-associated protein 35; Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The CSC seems to associate with the cytoplasmic domain of cargo proteins predominantly via VPS35; however, these interactions seem to be of low affinity and retromer SNX proteins may [...] (796 aa)
      
      0.705
RPUSD3
Mitochondrial mRNA pseudouridine synthase RPUSD3; Major enzyme responsible for the conversion of uridine to pseudouridine (PSI) at position 390 in mitochondrial COXI (MT- CO1) mRNA and at position 697-699 in mitochondrial COXIII (MT-CO3) mRNA, modulating the efficiency of mitochondrial protein synthesis without changes in transcript abundance or stability; Belongs to the pseudouridine synthase RluA family (351 aa)
   
 
  0.624
QTRTD1
Queuine tRNA-ribosyltransferase accessory subunit 2; Non-catalytic subunit of the queuine tRNA- ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1- yl)amino)methyl)-7-deazaguanosine) (427 aa)
   
 
  0.607
TRMT11
tRNA (guanine(10)-N2)-methyltransferase homolog; Catalytic subunit of an S-adenosyl-L-methionine- dependent tRNA methyltransferase complex that mediates the methylation of the guanosine nucleotide at position 10 (m2G10) in tRNAs (463 aa)
      
   
  0.599
RPUSD2
RNA pseudouridylate synthase domain containing 2 (545 aa)
   
 
  0.598
ZMYM3
Zinc finger MYM-type protein 3; Plays a role in the regulation of cell morphology and cytoskeletal organization; Zinc fingers MYM-type (1370 aa)
      
   
  0.584
RPUSD1
RNA pseudouridylate synthase domain containing 1; Belongs to the pseudouridine synthase RluA family (312 aa)
   
 
  0.570
TRMT112
Multifunctional methyltransferase subunit TRM112-like protein; Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with HEMK2/N6AMT1 catalyzes N5-methylation of ETF1 on ’Gln-185’, using S-adenosyl L- methionine as methyl donor. The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5- methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Involved in the pre-rRNA processing steps leading t [...] (125 aa)
      
      0.553
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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