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UBP7 protein (Saccharomyces cerevisiae) - STRING interaction network
"UBP7" - Ubiquitin-specific protease that cleaves ubiquitin-protein fusions in Saccharomyces cerevisiae
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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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UBP7Ubiquitin-specific protease that cleaves ubiquitin-protein fusions; Involved in the sorting of ubiquitinated cargo proteins at the multivesicular body (MVB) (1071 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)
       
 
  0.839
HSE1
Subunit of the endosomal Vps27p-Hse1p complex required for sorting of ubiquitinated membrane proteins into intralumenal vesicles prior to vacuolar degradation, as well as for recycling of Golgi proteins and formation of lumenal membranes; Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane (452 aa)
     
 
  0.800
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)
     
 
  0.755
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)
     
 
  0.726
UBP9
Ubiquitin carboxyl-terminal hydrolase, ubiquitin-specific protease that cleaves ubiquitin-protein fusions (754 aa)
       
 
  0.722
BBC1
Protein possibly involved in assembly of actin patches; interacts with an actin assembly factor Las17p and with the SH3 domains of Type I myosins Myo3p and Myo5p; localized predominantly to cortical actin patches; Involved in the regulation of actin cytoskeleton (1157 aa)
     
 
  0.711
PPR1
Zinc finger transcription factor containing a Zn(2)-Cys(6) binuclear cluster domain, positively regulates transcription of genes involved in uracil biosynthesis; activity may be modulated by interaction with Tup1p; Positive regulator of URA1 and URA3 expression (904 aa)
       
 
  0.700
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)
       
 
  0.694
RUB1
Ubiquitin-like protein with similarity to mammalian NEDD8; conjugation (neddylation) substrates include the cullins Cdc53p, Rtt101p, and Cul3p; activated by Ula1p and Uba3p (E1 enzyme pair); conjugation mediated by Ubc12p (E2 enzyme); Ubiquitin-like protein modifier that can be covalently attached to lysine residues of target proteins. Activated by the dimeric UBA3-ULA1 E1 enzyme and conjugated by the E2 UBC12 to substrate proteins. RUB1-conjugated (neddylated) substrate proteins include the cullins CDC53, RTT101 and CUL3, and the modification enhances the ubiquitin-ligase activity of [...] (77 aa)
       
 
  0.661
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)
       
 
  0.650
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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