• Version:
  • 11.0 [archived version]
STRINGSTRING
ADAR ADAR OARD1 OARD1 SAMHD1 SAMHD1 TREX1 TREX1 RNASEH2C RNASEH2C RNASEH2B RNASEH2B RNASEH2A RNASEH2A CCNB1 CCNB1 FEN1 FEN1 CCNB2 CCNB2 RNASEH1 RNASEH1
"RNASEH2C" - Ribonuclease H2 subunit C in Homo sapiens
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
RNASEH2CRibonuclease H2 subunit C; Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA-RNA duplexes (164 aa)    
Predicted Functional Partners:
RNASEH2B
Ribonuclease H2 subunit B; Non catalytic subunit of RNase H2, an endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA-RNA duplexes (312 aa)
     
  0.999
RNASEH2A
Ribonuclease H2 subunit A; Catalytic subunit of RNase HII, an endonuclease that specifically degrades the RNA of RNA-DNA hybrids. Participates in DNA replication, possibly by mediating the removal of lagging- strand Okazaki fragment RNA primers during DNA replication. Mediates the excision of single ribonucleotides from DNA-RNA duplexes; Belongs to the RNase HII family. Eukaryotic subfamily (299 aa)
     
  0.999
CCNB2
G2/mitotic-specific cyclin-B2; Essential for the control of the cell cycle at the G2/M (mitosis) transition; Belongs to the cyclin family. Cyclin AB subfamily (398 aa)
       
 
  0.842
CCNB1
G2/mitotic-specific cyclin-B1; Essential for the control of the cell cycle at the G2/M (mitosis) transition; Belongs to the cyclin family. Cyclin AB subfamily (433 aa)
       
 
  0.829
TREX1
Three-prime repair exonuclease 1; Major cellular 3’-to-5’ DNA exonuclease which digests single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) with mismatched 3’ termini. Prevents cell-intrinsic initiation of autoimmunity. Acts by metabolizing DNA fragments from endogenous retroelements, including L1, LTR and SINE elements. Unless degraded, these DNA fragments accumulate in the cytosol and activate the IFN-stimulatory DNA (ISD) response and innate immune signaling. Prevents chronic ATM-dependent checkpoint activation, by processing ssDNA polynucleotide species arising from the pro [...] (314 aa)
           
  0.748
SAMHD1
Deoxynucleoside triphosphate triphosphohydrolase SAMHD1; Host restriction nuclease involved in defense response to virus. Has dNTPase activity and reduces cellular dNTP levels to levels too low for retroviral reverse transcription to occur. Blocks early-stage virus replication in dendritic and other myeloid cells. Likewise, suppresses LINE-1 retrotransposon activity. May play a role in mediating proinflammatory responses to TNF-alpha signaling. Has ribonuclease activity, acting on single-stranded RNA. This activity is essential for H1V-1 restriction; Sterile alpha motif domain containing (626 aa)
           
  0.739
ADAR
Double-stranded RNA-specific adenosine deaminase; Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structur [...] (1226 aa)
           
  0.673
OARD1
O-acetyl-ADP-ribose deacetylase 1; Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O- acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP- ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively (152 aa)
     
        0.638
RNASEH1
Ribonuclease H1; Endonuclease that specifically degrades the RNA of RNA- DNA hybrids. Plays a role in RNA polymerase II (RNAp II) transcription termination by degrading R-loop RNA-DNA hybrid formation at G-rich pause sites located downstream of the poly(A) site and behind the elongating RNAp II; Belongs to the RNase H family (286 aa)
     
   
  0.631
FEN1
Flap endonuclease 1; Structure-specific nuclease with 5’-flap endonuclease and 5’-3’ exonuclease activities involved in DNA replication and repair. During DNA replication, cleaves the 5’-overhanging flap structure that is generated by displacement synthesis when DNA polymerase encounters the 5’-end of a downstream Okazaki fragment. It enters the flap from the 5’-end and then tracks to cleave the flap base, leaving a nick for ligation. Also involved in the long patch base excision repair (LP-BER) pathway, by cleaving within the apurinic/apyrimidinic (AP) site-terminated flap. Acts as a [...] (380 aa)
     
   
  0.563
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
Server load: low (0%) [HD]