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PUF2 protein (Saccharomyces cerevisiae) - STRING interaction network
"PUF2" - Member of the PUF protein family, which is defined by the presence of Pumilio homology domains that confer RNA binding activity in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
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protein homology
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PUF2Member of the PUF protein family, which is defined by the presence of Pumilio homology domains that confer RNA binding activity; preferentially binds mRNAs encoding membrane-associated proteins; RNA-binding protein involved in post-transcriptional regulation. Negatively regulates expression of COX17 by binding to the 3’-UTR of COX17 mRNA. Promotes decay of COX17 mRNA by enhancing its rate of deadenylation and subsequent turnover. Predominantly binds to mRNAs encoding membrane-associated proteins with roles in transmembrane transport and vesicular trafficking (1075 aa)    
Predicted Functional Partners:
PUF6
Pumilio-homology domain protein that binds the 3’ UTR of ASH1 mRNA and represses its translation, resulting in proper asymmetric localization of ASH1 mRNA; also co-sediments with the 60S ribosomal subunit and is required for its biogenesis; RNA-binding protein involved in post-transcriptional regulation. Component of the ASH1 mRNP which transports the ASH1 mRNA to the distal tip of the bud, where the ASH1 protein is translated and targeted to the daughter cell nucleus. Binds to the ASH1 3’-UTR containing the PUF consensus UUGU segment and represses its translation. This silencing of AS [...] (656 aa)
     
   
  0.823
NAM8
RNA binding protein, component of the U1 snRNP protein; mutants are defective in meiotic recombination and in formation of viable spores, involved in the formation of DSBs through meiosis-specific splicing of REC107 pre-mRNA; Nam8p regulon embraces /.../iotic pre-mRNAs of REC107, HFM1, AMA1 SPO22 and PCH2; the putative RNA binding domains RRM2 and RRM3 are required for Nam8p meiotic function; Acts as a suppressor of mitochondrial splicing deficiencies when overexpressed. Could be a non-essential component of the mitochondrial splicing machinery (523 aa)
       
 
  0.816
MUD1
U1 snRNP A protein, homolog of human U1-A; involved in nuclear mRNA splicing; Involved in nuclear mRNA splicing. The principal role of the U1A is to help fold or maintain U1 RNA in an active configuration. It is the first snRNP to interact with pre-mRNA. This interaction is required for the subsequent binding of U2 snRNP and the U4/U6/U5 tri-snRNP (298 aa)
       
 
  0.816
SHE2
RNA-binding protein that binds specific mRNAs and interacts with She3p; part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud; RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Recruits the MYO4-SHE3 complex to the ASH1 mRNA. Recruits also LOC1 and PUF6 to ASH1 mRNA, which are required for translational repression of this mRNA (246 aa)
       
 
  0.814
PMP2
Proteolipid associated with plasma membrane H(+)-ATPase (Pma1p); regulates plasma membrane H(+)-ATPase activity; nearly identical to PMP1 (43 aa)
       
 
  0.766
CBC2
Small subunit of the heterodimeric cap binding complex with Sto1p; interacts with Npl3p, possibly to package mRNA for export from the nucleus; may have a role in telomere maintenance; contains an RNA-binding motif; Component of the CBC complex, which binds co- transcriptionally to the cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The C [...] (208 aa)
       
 
  0.750
HEK2
RNA binding protein involved in asymmetric localization of ASH1 mRNA; represses translation of ASH1 mRNA, an effect reversed by Yck1p-dependent phosphoryation; regulates telomere position effect and length; similarity to hnRNP-K; RNA-binding protein involved in the correct localization of transcripts in the cell. RNA localization is a widespread mechanism for achieving localized protein synthesis. Required for the asymmetric localization to the daughter cell nucleus of the ASH1 transcript, coding for a specific repressor of transcription. Overexpression inhibits translation of the ASH1 [...] (381 aa)
     
 
  0.728
PUB1
Poly (A)+ RNA-binding protein, abundant mRNP-component protein that binds mRNA and is required for stability of many mRNAs; component of glucose deprivation induced stress granules, involved in P-body-dependent granule assembly; May be associated with hnRNA within the nucleus and remains associated during nucleocytoplasmic mRNA transport, once the proteins are in the cytoplasm, disassembly of PUB1-RNA complexes may occur prior to PAB1 binding and formation of a translationally competent RNP complex. Binds to polyadenylated RNA; prefers to bind poly(rU); binds to T-rich single-stranded DNA (453 aa)
     
 
  0.705
POP2
RNase of the DEDD superfamily, subunit of the Ccr4-Not complex that mediates 3’ to 5’ mRNA deadenylation; Acts as probably catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vitro, POP2 has 3’- exoribonuclease activity with a preference for poly(A) RNAs, but also degrades poly(U) and poly(C) RNAs. Is part of a glucose- sensing system involved in growth control in response to glucose availability (433 aa)
       
 
  0.688
MRN1
RNA-binding protein proposed to be involved in translational regulation; binds specific categories of mRNAs, including those that contain upstream open reading frames (uORFs) and internal ribosome entry sites (IRES); RNA-binding protein that binds specific categories of mRNAs, including those that contain upstream open reading frames (uORFs) and internal ribosome entry sites (IRES). Probably involved in translational regulation (612 aa)
     
 
  0.675
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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