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UBA4 protein (Saccharomyces cerevisiae) - STRING interaction network
"UBA4" - E1-like protein that activates Urm1p before urmylation in Saccharomyces cerevisiae
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experimentally determined
Predicted Interactions
gene neighborhood
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gene co-occurrence
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textmining
co-expression
protein homology
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UBA4E1-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)    
Predicted Functional Partners:
URM1
Ubiquitin-like protein involved in thiolation of cytoplasmic tRNAs; receives sulfur from the E1-like enzyme Uba4p and transfers it to tRNA; also functions as a protein tag with roles in nutrient sensing and oxidative stress response; Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2- thiolation reaction by being thiocarboxylated (-COSH) at its C- terminus by UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modifica [...] (99 aa)
       
  0.997
NFS1
Cysteine desulfurase involved in iron-sulfur cluster (Fe/S) biogenesis and in thio-modification of mitochondrial and cytoplasmic tRNAs; essential protein located predominantly in mitochondria; Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron- sulfur (Fe-S) clusters. Plays a role in both tRNA-processing and mitochondrial metabolism. Involved in the 2-thio-modification of both 5-carboxymethylaminomethyl-2-thiouridine in mitochondrial tRNAs and 5-methoxycarbonylmethyl-2-thiouridine (mcm5s2U) in cytoplasmic tRNAs (497 aa)
   
  0.993
RAD6
Ubiquitin-conjugating enzyme (E2), involved in postreplication repair (as a heterodimer with Rad18p), DSBR and checkpoint control (as a heterodimer with Bre1p), ubiquitin-mediated N-end rule protein degradation (as a heterodimer with Ubr1p; Catalyzes the covalent attachment of ubiquitin to other proteins. In association with the E3 enzyme BRE1 and LGE1, it plays a role in transcription regulation by catalyzing the monoubiquitination of histone H2B to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation, elongation by RNA polymerase II, telomeric si [...] (172 aa)
       
  0.993
TUM1
Rhodanese domain sulfur transferase, accepts persulfite from Nfs1p and transfers it to Uba4p in the pathway for 2-thiolation of the wobble uridine base of tRNAs; also stimulates sulfur transfer by Nfs1p; may be mitochondrially localized; Required for formation of the 2-thio group of the 5- methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs (304 aa)
     
  0.990
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)
     
  0.988
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)
       
  0.981
UBA3
Protein that activates Rub1p (NEDD8) before neddylation; acts together with Ula1p; may play a role in protein degradation; GFP-fusion protein localizes to the cytoplasm in a punctate pattern ; Catalytic subunit of the dimeric UBA3-ULA1 E1 enzyme. E1 activates NEDD8/RUB1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of UBC12 (299 aa)
 
 
0.976
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)
       
0.968
ATG7
Autophagy-related protein and dual specificity member of the E1 family of ubiquitin-activating enzymes; mediates the conjugation of Atg12p with Atg5p and Atg8p with phosphatidylethanolamine, required steps in autophagosome formation; E1-like activating enzyme involved in the 2 ubiquitin- like systems required for cytoplasm to vacuole transport (Cvt) and autophagy. Activates ATG12 for its conjugation with ATG5 and ATG8 for its conjugation with phosphatidylethanolamine. Both systems are needed for the ATG8 association to Cvt vesicles and autophagosomes membranes. Autophagy is essential f [...] (630 aa)
       
0.966
CDC53
Cullin, structural protein of SCF complexes (which also contain Skp1p, Cdc34p, Hrt1p and an F-box protein) involved in ubiquitination; SCF promotes the G1-S transition by targeting G1 cyclins and the Cln-CDK inhibitor Sic1p for degradation; Core component of multiple cullin-RING-based SCF (SKP1- CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The SCF complex associates w [...] (815 aa)
       
  0.945
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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