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UBC1 protein (Saccharomyces cerevisiae) - STRING interaction network
"UBC1" - Ubiquitin-conjugating enzyme that mediates selective degradation of short-lived and abnormal proteins 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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UBC1Ubiquitin-conjugating enzyme that mediates selective degradation of short-lived and abnormal proteins; plays a role in vesicle biogenesis and ER-associated protein degradation (ERAD); component of the cellular stress response; Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rap [...] (215 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)
     
 
  0.987
UBA1
Ubiquitin activating enzyme (E1), involved in ubiquitin-mediated protein degradation and essential for viability; Catalyzes the first step in ubiquitin conjugation to mark cellular proteins for degradation through the ubiquitin- proteasome system. Activates ubiquitin by first adenylating its C- terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP (1024 aa)
     
  0.980
RSP5
E3 ubiquitin ligase of the NEDD4 family; involved in regulating many cellular processes including MVB sorting, heat shock response, transcription, endocytosis, and ribosome stability; human homolog is involved in Liddle syndrome; mutant tolerates an /.../dy; ubiquitylates Sec23p; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Component of a RSP5 ubiquitin ligase complex which specifies polyubiquitination and intracellular trafficking of the general a [...] (809 aa)
     
  0.979
APC11
Catalytic core subunit, Anaphase-Promoting Complex/Cyclosome (APC/C); which is a ubiquitin-protein ligase required for degradation of anaphase inhibitors, including mitotic cyclins, during the metaphase/anaphase transition; contains a RING-H2 domain that is required for activity; Probably catalytic subunit of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin- protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin- conju [...] (165 aa)
     
  0.973
MMS2
Ubiquitin-conjugating enzyme variant involved in error-free postreplication repair; forms a heteromeric complex with Ubc13p, an active ubiquitin-conjugating enzyme; cooperates with chromatin-associated RING finger proteins, Rad18p and Rad5p; Has a role in the DNA error-free postreplication repair (PRR) pathway. Lacks catalytic activity by itself. The UBC13/MMS2 heterodimer catalyzes the synthesis of non-canonical poly- ubiquitin chains that are linked through ’Lys-63’ (137 aa)
     
  0.955
UBA4
E1-like protein that activates Urm1p before urmylation; also acts in thiolation of the wobble base of cytoplasmic tRNAs by adenylating and then thiolating Urm1p; receives sulfur from Tum1p; Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl- adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The re [...] (440 aa)
       
  0.937
UFD4
Ubiquitin-protein ligase (E3) that interacts with Rpt4p and Rpt6p, two subunits of the 19S particle of the 26S proteasome; cytoplasmic E3 involved in the degradation of ubiquitin fusion proteins; E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (1483 aa)
     
  0.929
SMT3
Ubiquitin-like protein of the SUMO family, conjugated to lysine residues of target proteins; regulates chromatid cohesion, chromosome segregation, APC-mediated proteolysis, DNA replication and septin ring dynamics; phosphorylated at Ser2; Not known; suppressor of MIF2 mutations (101 aa)
     
  0.916
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)
       
 
  0.915
ASR1
Ubiquitin ligase that modifies and regulates RNA Pol II; involved in a putative alcohol-responsive signaling pathway; accumulates in the nucleus under alcohol stress; contains a Ring/PHD finger domain similar to the mammalian rA9 protein; Required for tolerance to alcohol (288 aa)
     
 
  0.908
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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