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XRN2 protein (human) - STRING interaction network
"XRN2" - 5'-3' exoribonuclease 2 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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[Homology]
Score
XRN25’-3’ exoribonuclease 2; Possesses 5’->3’ exoribonuclease activity (By similarity). May promote the termination of transcription by RNA polymerase II. During transcription termination, cleavage at the polyadenylation site liberates a 5’ fragment which is subsequently processed to form the mature mRNA and a 3’ fragment which remains attached to the elongating polymerase. The processive degradation of this 3’ fragment by this protein may promote termination of transcription. Binds to RNA polymerase II (RNAp II) transcription termination R-loops formed by G-rich pause sites (PubMed-21700224) (950 aa)    
Predicted Functional Partners:
DOM3Z
Dom-3 homolog Z (C. elegans); Ribonuclease that specifically degrades pre-mRNAs with a defective 5’ end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5’-3’ exonuclease activities. Has decapping activity toward incomplete 5’ end cap mRNAs such as unmethylated 5’ end-capped RNA to release GpppN and 5’ end monophosphate RNA. The 5’ end monophosphate RNA is then degraded by the 5’-3’ exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5’-pyrophosphohydrolase activity by hydrolyzin [...] (396 aa)
     
 
  0.995
DCP2
DCP2 decapping enzyme homolog (S. cerevisiae); Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed-12417715, PubMed-12218187, PubMed-12923261, PubMed-21070968). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5’-phosphorylated mRNA fragment and 7m-GDP (PubMed-12486012, PubMed-12923261, PubMed-21070968). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed-14527413). Plays a role in replication-dependent histone mRNA degradation (PubMed-18172165). Has higher activ [...] (420 aa)
     
 
  0.955
FBL
Fibrillarin; S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2’-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of ’Gln-105’ of histone H2A (H2AQ104me), a modification that impairs binding of the [...] (321 aa)
     
  0.949
NOP58
NOP58 ribonucleoprotein homolog (yeast); Required for 60S ribosomal subunit biogenesis (By similarity). Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such as U3, U8 and U14 snoRNAs (529 aa)
     
  0.946
NOP56
NOP56 ribonucleoprotein homolog (yeast); Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (594 aa)
     
  0.944
PDCD11
Programmed cell death 11; Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA (1871 aa)
     
 
  0.939
DDX52
DEAD (Asp-Glu-Ala-Asp) box polypeptide 52 (599 aa)
     
  0.935
RPS8
Ribosomal protein S8 (208 aa)
     
  0.928
RPS4X
Ribosomal protein S4, X-linked (263 aa)
     
  0.927
RPS4Y2
Ribosomal protein S4, Y-linked 2 (263 aa)
     
  0.927
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo, Homo sapiens, human, man
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