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  • 11.0 [archived version]
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RIF1 RIF1 FAM124A FAM124A RNASEH2B RNASEH2B AP1M1 AP1M1 SAMHD1 SAMHD1 TREX1 TREX1 RNASEH2A RNASEH2A ADAR ADAR RNASEH2C RNASEH2C PCNA PCNA FEN1 FEN1
"RNASEH2B" - Ribonuclease H2 subunit B in Homo sapiens
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query proteins and first shell of interactors
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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
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textmining
co-expression
protein homology
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RNASEH2BRibonuclease 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)    
Predicted Functional Partners:
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
RNASEH2C
Ribonuclease 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)
     
  0.999
PCNA
Proliferating cell nuclear antigen; Auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase’s processibility during elongation of the leading strand. Induces a robust stimulatory effect on the 3’- 5’ exonuclease and 3’-phosphodiesterase, but not apurinic- apyrimidinic (AP) endonuclease, APEX2 activities. Has to be loaded onto DNA in order to be able to stimulate APEX2. Plays a key role in DNA damage response (DDR) by being conveniently positioned at the replication fork to coordinate DNA replication with DNA re [...] (261 aa)
     
 
  0.975
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)
     
   
  0.860
AP1M1
AP-1 complex subunit mu-1; Subunit of clathrin-associated adaptor protein complex 1 that plays a role in protein sorting in the trans-Golgi network (TGN) and endosomes. The AP complexes mediate the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (435 aa)
       
      0.847
FAM124A
Protein FAM124A; Family with sequence similarity 124 member A; Belongs to the FAM124 family (582 aa)
           
  0.750
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
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)
     
   
  0.684
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)
     
 
  0.669
RIF1
Telomere-associated protein RIF1; Key regulator of TP53BP1 that plays a key role in the repair of double-strand DNA breaks (DSBs) in response to DNA damage- acts by promoting non-homologous end joining (NHEJ)- mediated repair of DSBs. In response to DNA damage, interacts with ATM-phosphorylated TP53BP1. Interaction with TP53BP1 leads to dissociate the interaction between NUDT16L1/TIRR and TP53BP1, thereby unmasking the tandem Tudor-like domain of TP53BP1 and allowing recruitment to DNA DSBs. Once recruited to DSBs, RIF1 and TP53BP1 act by promoting NHEJ-mediated repair of DSBs. In the [...] (2472 aa)
     
        0.645
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, Homo sapiens, human, man
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