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UBA3 protein (Saccharomyces cerevisiae) - STRING interaction network
"UBA3" - Protein that activates Rub1p in Saccharomyces cerevisiae
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UBA3Protein 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)    
Predicted Functional Partners:
ULA1
Protein that activates Rub1p (NEDD8) before neddylation; acts together with Uba3p; may play a role in protein degradation; Regulatory 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 (462 aa)
     
 
  0.999
UBC12
Enzyme that mediates the conjugation of Rub1p, a ubiquitin-like protein, to other proteins; related to E2 ubiquitin-conjugating enzymes; Accepts the ubiquitin-like protein NEDD8/RUB1 from the UBA3-ULA1 E1 complex and catalyzes its covalent attachment to other proteins. The major substrate is CDC53/Cullin (188 aa)
     
  0.998
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)
       
  0.996
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)
       
  0.994
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)
     
  0.994
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)
     
  0.988
HRT1
RING finger containing subunit of Skp1-Cullin-F-box ubiquitin protein ligases (SCF); required for Gic2p, Far1p, Sic1p and Cln2p degradation; may tether Cdc34p (a ubiquitin conjugating enzyme or E2) and Cdc53p (a cullin) subunits of SCF; Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes (CRLs), which mediate the ubiquitination of target proteins. Recruits the E2 ubiquitin- conjugating enzyme CDC34/UBC3 to the complex and brings it into close proximity to the substrate. Also stimulates CDC34/UBC3 autoubiquitination and promotes the neddylation of CDC53 an [...] (121 aa)
     
 
  0.984
SKP1
Evolutionarily conserved kinetochore protein that is part of multiple protein complexes, including the SCF ubiquitin ligase complex, the CBF3 complex that binds centromeric DNA, and the RAVE complex that regulates assembly of the V-ATPase; Essential component of the E3 ubiquitin ligase complex SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination and subsequent proteasomal degradation of target proteins like phosphorylated SIC1. Participates in the attachment of chromosomes to the spindle. Acts as a regulatory component of the centromere DNA-binding [...] (194 aa)
     
 
  0.980
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)
 
 
0.976
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)
       
  0.976
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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