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UBP1 ubiquitin-specific protease UBP1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 851435, updated on 2-Nov-2024

Summary

Official Symbol
UBP1
Official Full Name
ubiquitin-specific protease UBP1
Primary source
SGD:S000002280
Locus tag
YDL122W
See related
AllianceGenome:SGD:S000002280; FungiDB:YDL122W; VEuPathDB:YDL122W
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary
Enables cysteine-type deubiquitinase activity. Involved in protein deubiquitination. Located in endoplasmic reticulum. Is active in endoplasmic reticulum membrane. Orthologous to human USP30 (ubiquitin specific peptidase 30). [provided by Alliance of Genome Resources, Nov 2024]
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Genomic context

See UBP1 in Genome Data Viewer
Location:
chromosome: IV
Exon count:
1
Sequence:
Chromosome: IV; NC_001136.10 (242552..244981)

Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene aldo-keto reductase superfamily protein Neighboring gene Sna4p Neighboring gene Exp1p Neighboring gene ferroxidase

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables cysteine-type deubiquitinase activity IBA
Inferred from Biological aspect of Ancestor
more info
 
enables cysteine-type deubiquitinase activity IDA
Inferred from Direct Assay
more info
PubMed 
enables cysteine-type deubiquitinase activity IEA
Inferred from Electronic Annotation
more info
 
enables cysteine-type peptidase activity IEA
Inferred from Electronic Annotation
more info
 
enables zinc ion binding RCA
inferred from Reviewed Computational Analysis
more info
PubMed 
Process Evidence Code Pubs
involved_in protein deubiquitination IDA
Inferred from Direct Assay
more info
PubMed 
involved_in protein deubiquitination IEA
Inferred from Electronic Annotation
more info
 
involved_in proteolysis IEA
Inferred from Electronic Annotation
more info
 
involved_in regulation of protein stability IBA
Inferred from Biological aspect of Ancestor
more info
 
Component Evidence Code Pubs
located_in cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in cytosol IBA
Inferred from Biological aspect of Ancestor
more info
 
located_in endoplasmic reticulum HDA PubMed 
located_in endoplasmic reticulum IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in endoplasmic reticulum membrane IDA
Inferred from Direct Assay
more info
PubMed 
is_active_in nucleus IBA
Inferred from Biological aspect of Ancestor
more info
 

General protein information

Preferred Names
ubiquitin-specific protease UBP1
NP_010161.1
  • Ubiquitin-specific protease; removes ubiquitin from ubiquitinated proteins; cleaves at the C terminus of ubiquitin fusions irrespective of their size; capable of cleaving polyubiquitin chains

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001136.10 Reference assembly

    Range
    242552..244981
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001180181.1NP_010161.1  TPA: ubiquitin-specific protease UBP1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_010161.1

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VRM8, P25037, Q07543
    UniProtKB/TrEMBL
    C7GJJ4, N1PA89
    Conserved Domains (2) summary
    cd02662
    Location:102736
    Peptidase_C19F; A subfamily of Peptidase C19. Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyze bonds involving the carboxyl ...
    cl02553
    Location:101293
    Peptidase_C19; Peptidase C19 contains ubiquitinyl hydrolases. They are intracellular peptidases that remove ubiquitin molecules from polyubiquinated peptides by cleavage of isopeptide bonds. They hydrolyse bonds involving the carboxyl group of the C-terminal Gly ...