Q04638 · ITT1_YEAST
- ProteinE3 ubiquitin-protein ligase ITT1
- GeneITT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids464 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
E3 ubiquitin-protein ligase involved in translation quality control (PubMed:11570975, PubMed:37951215).
Involved in the rescue of stalled ribosomes by promoting ubiquitination and degradation of proteins on stalled ribosomes (PubMed:37951215).
Specifically required to resolve RNA-protein cross-links caused by reactive aldehydes, which trigger translation stress by stalling ribosomes: acts by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, leading to their degradation (PubMed:37951215).
Interacts with the translation termination factors eRF1 (SUP45) and eRF3 (SUP35); overexpression decreases the efficiency of translation termination (PubMed:11570975).
Involved in the rescue of stalled ribosomes by promoting ubiquitination and degradation of proteins on stalled ribosomes (PubMed:37951215).
Specifically required to resolve RNA-protein cross-links caused by reactive aldehydes, which trigger translation stress by stalling ribosomes: acts by catalying 'Lys-6'-linked ubiquitination of RNA-protein cross-links, leading to their degradation (PubMed:37951215).
Interacts with the translation termination factors eRF1 (SUP45) and eRF3 (SUP35); overexpression decreases the efficiency of translation termination (PubMed:11570975).
Miscellaneous
Present with 846 molecules/cell in log phase SD medium.
Catalytic activity
Pathway
Protein modification; protein ubiquitination.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 180 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 183 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 210 | Zn2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 290 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 300 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 316 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 319 | Zn2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 402 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 405 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Active site | 415 | |||||
Sequence: C | ||||||
Binding site | 420 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 423 | Zn2+ 3 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 428 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 431 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 443 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 451 | Zn2+ 4 (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | ubiquitin ligase complex | |
Molecular Function | ubiquitin conjugating enzyme binding | |
Molecular Function | ubiquitin protein ligase activity | |
Molecular Function | zinc ion binding | |
Biological Process | protein K6-linked ubiquitination | |
Biological Process | protein polyubiquitination | |
Biological Process | protein-RNA covalent cross-linking repair | |
Biological Process | regulation of translational termination | |
Biological Process | rescue of stalled ribosome | |
Biological Process | ubiquitin-dependent protein catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameE3 ubiquitin-protein ligase ITT1
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Saccharomycotina > Saccharomycetes > Saccharomycetales > Saccharomycetaceae > Saccharomyces
Accessions
- Primary accessionQ04638
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000056340 | 1-464 | E3 ubiquitin-protein ligase ITT1 | |||
Sequence: MALTQFENDLEILRDMYPELEMKSVKVEEEGEFPQRINGKLLFKISLLADVNIEFGEQHMLLSNLSNECVEFTIYSCHYPDIRRCVVMDIKSLWISTDEKKMLIDKALRLVEETVDMSIEFADSFTSILILIFGFLIDDTAILLFPNGIRKCLTQDQYDLFKQISEEATLQKVSRSNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKCGKKVSLSTDIIEEYLDDTVTSYERKRKLEAKYGRRVLELEVNDYLAEKMLDLAIKKEGSNLQRCPKCKVVVERSEGCNKMKCEVCGTLFCFICGVLLYPEDPYEHFREAYSGCYGRLFEGMPGTET |
Proteomic databases
PTM databases
Interaction
Subunit
Interacts with translation release factors eRF1 (SUP45) and eRF3 (SUP35) in vitro.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q04638 | SUP35 P05453 | 3 | EBI-27858, EBI-6540 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 176-455 | TRIAD supradomain | ||||
Sequence: SNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKCGKKVSLSTDIIEEYLDDTVTSYERKRKLEAKYGRRVLELEVNDYLAEKMLDLAIKKEGSNLQRCPKCKVVVERSEGCNKMKCEVCGTLFCFICGVLLYPEDPYEHFREAYSGCYGRL | ||||||
Zinc finger | 180-236 | RING-type 1 | ||||
Sequence: CCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKE | ||||||
Zinc finger | 267-338 | IBR-type | ||||
Sequence: DTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKC | ||||||
Zinc finger | 402-431 | RING-type 2; atypical | ||||
Sequence: CPKCKVVVERSEGCNKMKCEVCGTLFCFIC |
Domain
Members of the RBR family are atypical E3 ligases. They interact with the E2 conjugating enzyme UBE2L3 and function like HECT-type E3 enzymes: they bind E2s via the first RING domain, but require an obligate trans-thiolation step during the ubiquitin transfer, requiring a conserved cysteine residue in the second RING domain.
Sequence similarities
Belongs to the RBR family. RNF14 subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length464
- Mass (Da)54,096
- Last updated1997-11-01 v1
- ChecksumF481372B742AF63D
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z38114 EMBL· GenBank· DDBJ | CAA86252.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BK006946 EMBL· GenBank· DDBJ | DAA09829.1 EMBL· GenBank· DDBJ | Genomic DNA |