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ITT1 protein (Saccharomyces cerevisiae) - STRING interaction network
"ITT1" - Protein that modulates the efficiency of translation termination, interacts with translation release factors eRF1 in Saccharomyces cerevisiae
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ITT1Protein that modulates the efficiency of translation termination, interacts with translation release factors eRF1 (Sup45p) and eRF3 (Sup35p) in vitro, contains a zinc finger domain characteristic of the TRIAD class of proteins; Modulates the efficiency of translation termination, resulting in the readthrough of all three types of nonsense codons UAA, UAG and UGA (464 aa)    
Predicted Functional Partners:
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)
       
    0.912
MPE1
Essential conserved subunit of CPF (cleavage and polyadenylation factor), plays a role in 3’ end formation of mRNA via the specific cleavage and polyadenylation of pre-mRNA, contains a putative RNA-binding zinc knuckle motif; Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3’-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB (441 aa)
     
    0.905
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)
     
 
    0.902
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)
     
 
    0.902
HRT3
Putative SCF-ubiquitin ligase F-box protein, based on both genetic and physical interactions and sequence similarity; identified in association with Cdc53p, Skp1p and Ubi4 in large and small-scale studies; Substrate recognition component of a SCF (SKP1-CUL1-F- box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Probably recognizes and binds to phosphorylated target proteins (By similarity) (344 aa)
     
 
    0.901
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)
     
 
    0.901
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)
         
  0.901
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)
     
 
    0.900
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)
         
    0.900
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)
         
    0.900
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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