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UBP14 protein (Saccharomyces cerevisiae) - STRING interaction network
"UBP14" - Ubiquitin-specific protease in Saccharomyces cerevisiae
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Known Interactions
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experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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UBP14Ubiquitin-specific protease; specifically disassembles unanchored ubiquitin chains; involved in fructose-1,6-bisphosphatase (Fbp1p) degradation; similar to human isopeptidase T; Has a role in the negative regulation of gluconeogenesis. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome (781 aa)    
Predicted Functional Partners:
UBI4
Ubiquitin, becomes conjugated to proteins, marking them for selective degradation via the ubiquitin-26S proteasome system; essential for the cellular stress response; encoded as a polyubiquitin precursor comprised of 5 head-to-tail repeats; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiqui [...] (381 aa)
     
  0.992
UBP3
Ubiquitin-specific protease involved in transport and osmotic response; interacts with Bre5p to co-regulate anterograde and retrograde transport between the ER and Golgi; involved in transcription elongation in response to osmostress through phospho /.../on at Ser695 by Hog1p; inhibitor of gene silencing; cleaves ubiquitin fusions but not polyubiquitin; also has mRNA binding activity; Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-termina [...] (912 aa)
     
  0.963
RPS31
Fusion protein that is cleaved to yield a ribosomal protein of the small (40S) subunit and ubiquitin; ubiquitin may facilitate assembly of the ribosomal protein into ribosomes; interacts genetically with translation factor eIF2B; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear [...] (152 aa)
     
  0.947
RPL40B
Fusion protein, identical to Rpl40Ap, that is cleaved to yield ubiquitin and a ribosomal protein of the large (60S) ribosomal subunit with similarity to rat L40; ubiquitin may facilitate assembly of the ribosomal protein into ribosomes; Ubiquitin- exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin [...] (128 aa)
     
  0.930
VPS30
Subunit of phosphatidylinositol (PtdIns) 3-kinase complexes I and II; Complex I is essential in autophagy and Complex II is required for vacuolar protein sorting; ortholog of the higher eukaryotic gene Beclin 1; Required for cytoplasm to vacuole transport (Cvt), autophagy, nucleophagy, and mitophagy, as a part of the autophagy- specific VPS34 PI3-kinase complex I. This complex is essential to recruit the ATG8-phosphatidylinositol conjugate and the ATG12-ATG5 conjugate to the pre-autophagosomal structure. Also involved in endosome-to-Golgi retrograde transport as part of the VPS34 PI3- [...] (557 aa)
     
 
  0.900
UBP15
Ubiquitin-specific protease involved in protein deubiquitination; catalytic activity regulated by an N-terminal TRAF-like domain and and C-terminal sequences; physically interacts with anaphase-promoting complex/cyclosome (APC/C) activator, Cdh1p (1230 aa)
     
 
  0.838
UBP6
Ubiquitin-specific protease situated in the base subcomplex of the 26S proteasome, releases free ubiquitin from branched polyubiquitin chains; works in opposition to Hul5p polyubiquitin elongation activity; mutant has aneuploidy tolerance; Predominant proteasome-associated deubiquitinase which releases ubiquitin from the proteasome targeted ubiquitinated proteins. Ensures the regeneration of ubiquitin at the proteasome. Has proteasome-inhibitory activity and delays the degradation of ubiquitinated proteins to provide a time window allowing gradual deubiquitination of the substrate. Sta [...] (499 aa)
     
   
  0.820
UBP2
Ubiquitin-specific protease that removes ubiquitin from ubiquitinated proteins; interacts with Rsp5p and is required for MVB sorting of membrane proteins; can cleave polyubiquitin and has isopeptidase activity; Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety in natural or engineered linear fusion proteins, irrespective of their size or the presence of an N-terminal extension to ubiquitin. Removes ubiquitin chains that initiate proteolysis of FZO1 and inhibit mitochondrial fusion (1272 aa)
     
 
  0.792
YUH1
Ubiquitin C-terminal hydrolase; cleaves ubiquitin-protein fusions to generate monomeric ubiquitin; hydrolyzes the peptide bond at the C-terminus of ubiquitin; also the major processing enzyme for the ubiquitin-like protein Rub1p; Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or RUB1. Preferentially cleaves ubiquitin from peptides and small adducts (236 aa)
     
 
  0.791
PRE2
Beta 5 subunit of the 20S proteasome, responsible for the chymotryptic activity of the proteasome; The proteasome degrades poly-ubiquitinated proteins in the cytoplasm and in the nucleus. It is essential for the regulated turnover of proteins and for the removal of misfolded proteins. The proteasome is a multicatalytic proteinase complex that is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. It has an ATP-dependent proteolytic activity. This unit is responsible of the chymotrypsin-like acti [...] (287 aa)
     
 
  0.779
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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