Q04638 · ITT1_YEAST

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).

Miscellaneous

Present with 846 molecules/cell in log phase SD medium.

Caution

Lacks the His residue in the RING-type domain 2 that is one of the conserved features of the family.

Catalytic activity

  • [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine.
    EC:2.3.2.31 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site180Zn2+ 1 (UniProtKB | ChEBI)
Binding site183Zn2+ 1 (UniProtKB | ChEBI)
Binding site207Zn2+ 1 (UniProtKB | ChEBI)
Binding site210Zn2+ 1 (UniProtKB | ChEBI)
Binding site290Zn2+ 2 (UniProtKB | ChEBI)
Binding site300Zn2+ 2 (UniProtKB | ChEBI)
Binding site316Zn2+ 2 (UniProtKB | ChEBI)
Binding site319Zn2+ 2 (UniProtKB | ChEBI)
Binding site402Zn2+ 3 (UniProtKB | ChEBI)
Binding site405Zn2+ 3 (UniProtKB | ChEBI)
Active site415
Binding site420Zn2+ 3 (UniProtKB | ChEBI)
Binding site423Zn2+ 3 (UniProtKB | ChEBI)
Binding site428Zn2+ 4 (UniProtKB | ChEBI)
Binding site431Zn2+ 4 (UniProtKB | ChEBI)
Binding site443Zn2+ 4 (UniProtKB | ChEBI)
Binding site451Zn2+ 4 (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcytoplasm
Cellular Componentubiquitin ligase complex
Molecular Functionubiquitin conjugating enzyme binding
Molecular Functionubiquitin protein ligase activity
Molecular Functionzinc ion binding
Biological Processprotein K6-linked ubiquitination
Biological Processprotein polyubiquitination
Biological Processprotein-RNA covalent cross-linking repair
Biological Processregulation of translational termination
Biological Processrescue of stalled ribosome
Biological Processubiquitin-dependent protein catabolic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase ITT1
  • EC number

Gene names

    • Name
      ITT1
    • Ordered locus names
      YML068W

Organism names

Accessions

  • Primary accession
    Q04638
  • Secondary accessions
    • D6VZA5

Proteomes

Organism-specific databases

Subcellular Location

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00000563401-464E3 ubiquitin-protein ligase ITT1

Proteomic databases

PTM databases

Interaction

Subunit

Interacts with translation release factors eRF1 (SUP45) and eRF3 (SUP35) in vitro.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q04638SUP35 P054533EBI-27858, EBI-6540

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, zinc finger.

TypeIDPosition(s)Description
Region176-455TRIAD supradomain
Zinc finger180-236RING-type 1
Zinc finger267-338IBR-type
Zinc finger402-431RING-type 2; atypical

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    464
  • Mass (Da)
    54,096
  • Last updated
    1997-11-01 v1
  • Checksum
    F481372B742AF63D
MALTQFENDLEILRDMYPELEMKSVKVEEEGEFPQRINGKLLFKISLLADVNIEFGEQHMLLSNLSNECVEFTIYSCHYPDIRRCVVMDIKSLWISTDEKKMLIDKALRLVEETVDMSIEFADSFTSILILIFGFLIDDTAILLFPNGIRKCLTQDQYDLFKQISEEATLQKVSRSNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCHFVFCFDCLHAWHGYNNKCGKKVSLSTDIIEEYLDDTVTSYERKRKLEAKYGRRVLELEVNDYLAEKMLDLAIKKEGSNLQRCPKCKVVVERSEGCNKMKCEVCGTLFCFICGVLLYPEDPYEHFREAYSGCYGRLFEGMPGTET

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
Z38114
EMBL· GenBank· DDBJ
CAA86252.1
EMBL· GenBank· DDBJ
Genomic DNA
BK006946
EMBL· GenBank· DDBJ
DAA09829.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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