GO_REF:0000002

Gene Ontology annotation through association of InterPro records with GO terms

GO_REF:0000015

Use of the ND evidence code for Gene Ontology (GO) terms

GO_REF:0000033

Annotation inferences using phylogenetic trees

GO_REF:0000120

Combined Automated Annotation using Multiple IEA Methods

PMID:10527495

Chemically synthesized ubiquitin extension proteins detect distinct catalytic capacities of deubiquitinating enzymes.

Recombinant yeast Ubp11p was among the DUBs assayed against synthetic ubiquitin substrates and cleaved ubiquitin fusions, but isopeptidase activity was associated only with a different subset (Yuh1p, Unp, Ubp1p, Ubp2p), so UBP11's physiological linkage specificity is not defined here.

PMID:11076031

Analysis of the deubiquitinating enzymes of the yeast Saccharomyces cerevisiae.

All 17 yeast DUB genes were individually deleted; none of the single mutants is lethal or strongly growth-defective under standard conditions, and 14 of 17 DUBs (including Ubp11p) have demonstrated ubiquitin-cleaving activity — establishing both the DUB activity and the lack of a strong single-deletion phenotype for UBP11.

PMID:30358795

The cellular economy of the Saccharomyces cerevisiae zinc proteome.

A genome-wide bioinformatic + proteomic survey of the yeast zinc proteome; the source of the computational (RCA) zinc-ion-binding prediction for UBP11. Not a direct measurement of zinc binding by UBP11.

file:yeast/UBP11/UBP11-bioinformatics/RESULTS.md

UBP11 USP catalytic-domain integrity analysis (this repository)

Reproducible parse of the UniProt record confirms the USP catalytic dyad (nucleophile Cys307, proton acceptor His649) is intact within a 410-aa peptidase C19 domain, supporting a catalytically competent deubiquitinase.