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protein coding gene - uch2 (SPBC409.06) - ubiquitin C-terminal hydrolase Uch2

Gene summary

Standard name
uch2
Systematic ID
SPBC409.06
Product
ubiquitin C-terminal hydrolase Uch2
Organism
Schizosaccharomyces pombe (fission yeast)
UniProt ID
Q9UUB6
ORFeome ID
16/16B04
Characterisation status
biological role published
Feature type
mRNA gene
Genomic location
chromosome II: 1142192..1143522 forward strand

Annotation

GO biological process

GO:0071629 - cytoplasm protein quality control by the ubiquitin-proteasome system

References:

GO:0000338 - protein deneddylation

References:

GO cellular component

GO:0005737 - cytoplasm

References:

GO:0034399 - nuclear periphery

References:

GO:0005634 - nucleus

References:

GO:0000502 - proteasome complex

References:

GO molecular function

GO:0004843 - cysteine-type deubiquitinase activity

References:

GO:0019784 - deNEDDylase activity

References:

GO:0140492 - metal-dependent deubiquitinase activity

References:

Modification

MOD:00046 - O-phospho-L-serine

References:

MOD:00047 - O-phospho-L-threonine

References:

MOD:01148 - ubiquitinylated lysine

References:

Multi-locus phenotype

FYPO:0005822 - decreased NEDD8-specific protease activity

References:

Genotypes:

FYPO:0005818 - normal protein neddylation

References:

Genotypes:

FYPO:0002060 - viable vegetative cell population

References:

Genotypes:

Qualitative gene expression

PomGeneEx:0000019 - protein level decreased

References:

Quantitative gene expression

PBO:0006310 - protein level

References:

PBO:0011963 - RNA level

References:

Single locus phenotype

FYPO:0009073 - decreased cell population growth on lysine nitrogen source

References:

Genotypes:

FYPO:0001355 - decreased vegetative cell population growth

References:

Genotypes:

FYPO:0001023 - normal growth on cisplatin

References:

Genotypes:

FYPO:0005818 - normal protein neddylation

References:

Genotypes:

FYPO:0000067 - resistance to brefeldin A

References:

Genotypes:

FYPO:0000763 - resistance to cadmium

References:

Genotypes:

FYPO:0002693 - resistance to diamide

References:

Genotypes:

FYPO:0009038 - resistance to egtazic acid

References:

Genotypes:

FYPO:0001583 - resistance to lithium

References:

Genotypes:

FYPO:0009083 - resistance to lithium chloride and methyl methanesulfonate

References:

Genotypes:

FYPO:0009085 - resistance to lithium chloride and sodium dodecyl sulfate

References:

Genotypes:

FYPO:0003383 - resistance to tert-butyl hydroperoxide

References:

Genotypes:

FYPO:0000830 - resistance to vanadate

References:

Genotypes:

FYPO:0007921 - sensitive to benzamidine

References:

Genotypes:

FYPO:0001701 - sensitive to bortezomib

References:

Genotypes:

FYPO:0000104 - sensitive to cycloheximide

References:

Genotypes:

FYPO:0000842 - sensitive to ethanol during vegetative growth

References:

Genotypes:

FYPO:0007924 - sensitive to potassium chloride and sodium dodecyl sulfate

References:

Genotypes:

FYPO:0002060 - viable vegetative cell population

References:

Genotypes:

FYPO:0002177 - viable vegetative cell with normal cell morphology

References:

Genotypes:

Taxonomic conservation

PBO:0011065 - conserved in eukaryotes

PBO:0011071 - conserved in eukaryotes only

PBO:0011064 - conserved in fungi

PBO:0011069 - conserved in metazoa

PBO:0011070 - conserved in vertebrates

PBO:0000055 - no apparent S. cerevisiae ortholog

PBO:0006222 - predominantly single copy (one to one)

Protein features

IDNameInterPro nameDB name
PF18031UCH_CUCH_CPFAM
PF01088Peptidase_C12Peptidase_C12_UCHPFAM
cd09617Peptidase_C12_UCH37_BAP1CDD
PS52049ULDPROSITE_PROFILES
PS52048UCH_DOMAINPeptidase_C12_UCHPROSITE_PROFILES
PR00707UBCTHYDRLASEPeptidase_C12_UCHPRINTS
G3DSA:3.40.532.10:FF:000003FUNFAM
SSF54001Cysteine proteinasesPapain-like_cys_pep_sfSUPERFAMILY
G3DSA:3.40.532.10Peptidase_C12_UCH_sfGENE3D
G3DSA:1.20.58.860GENE3D
PTHR10589UBIQUITIN CARBOXYL-TERMINAL HYDROLASEPeptidase_C12_UCHPANTHER
PIRSF038120UchUbiquitinyl_hydrolase_UCH37PIRSF

Orthologs

References / Literature

PMID:30355493 - Expanded Interactome of the Intrinsically Disordered Protein Dss1.
Schenstrøm SM et al. Cell Rep 2018 Oct 23;25(4):862-870
PMID:22681890 - Hierarchical modularity and the evolution of genetic interactomes across species.
Ryan CJ et al. Mol Cell 2012 Jun 08;46(5):691-704
PMID:20838651 - A global census of fission yeast deubiquitinating enzyme localization and interaction networks reveals distinct compartmentalization profiles and overlapping functions in endocytosis and polarity.
Kouranti I et al. PLoS Biol 2010 Sep 07;8(9)
PMID:20133687 - Synergistic roles of the proteasome and autophagy for mitochondrial maintenance and chronological lifespan in fission yeast.
Takeda K et al. Proc Natl Acad Sci U S A 2010 Feb 23;107(8):3540-5
PMID:23101633 - Quantitative analysis of fission yeast transcriptomes and proteomes in proliferating and quiescent cells.
Marguerat S et al. Cell 2012 Oct 26;151(3):671-83
PMID:16149916 - Fission yeast Dss1 associates with the proteasome and is required for efficient ubiquitin-dependent proteolysis.
Jossé L et al. Biochem J 2006 Jan 01;393(Pt 1):303-9
PMID:23697806 - A genome-wide resource of cell cycle and cell shape genes of fission yeast.
Hayles J et al. Open Biol 2013 May 22;3(5):130053
PMID:26412298 - A Degenerate Cohort of Yeast Membrane Trafficking DUBs Mediates Cell Polarity and Survival.
Beckley JR et al. Mol Cell Proteomics 2015 Dec;14(12):3132-41
PMID:34496258 - Transcription and chromatin-based surveillance mechanism controls suppression of cryptic antisense transcription.
Heo DH et al. Cell Rep 2021 Sep 07;36(10):109671
PMID:30726745 - Fission Yeast NDR/LATS Kinase Orb6 Regulates Exocytosis via Phosphorylation of the Exocyst Complex.
Tay YD et al. Cell Rep 2019 Feb 05;26(6):1654-1667.e7
PMID:23496905 - Nedd8 processing enzymes in Schizosaccharomyces pombe.
O'Donoghue JE et al. BMC Biochem 2013 Mar 15;14:8
PMID:37970674 - SUMOylation regulates Lem2 function in centromere clustering and silencing.
Strachan J et al. J Cell Sci 2023 Dec 01;136(23)
PMID:21247416 - Ubiquitin-proteasome genes as targets for modulation of cisplatin sensitivity in fission yeast.
Gatti L et al. BMC Genomics 2011 Jan 19;12:44
GO_REF:0000033 - Annotation inferences using phylogenetic trees
PMID:22540037 - Predicting the fission yeast protein interaction network.
Pancaldi V et al. G3 (Bethesda) 2012 Apr;2(4):453-67
PMID:18257517 - Phosphoproteome analysis of fission yeast.
Wilson-Grady JT et al. J Proteome Res 2008 Mar;7(3):1088-97
PMID:33823663 - A TOR (target of rapamycin) and nutritional phosphoproteome of fission yeast reveals novel targets in networks conserved in humans.
Halova L et al. Open Biol 2021 Apr;11(4):200405
PMID:21511999 - Comparative functional genomics of the fission yeasts.
Rhind N et al. Science 2011 May 20;332(6032):930-6
PMID:20967237 - Fission yeast cells undergo nuclear division in the absence of spindle microtubules.
Castagnetti S et al. PLoS Biol 2010 Oct 12;8(10):e1000512
PMID:20473289 - Analysis of a genome-wide set of gene deletions in the fission yeast Schizosaccharomyces pombe.
Kim DU et al. Nat Biotechnol 2010 Jun;28(6):617-623
PMID:39705284 - Proteomic and phosphoproteomic analyses reveal that TORC1 is reactivated by pheromone signaling during sexual reproduction in fission yeast.
Bérard M et al. PLoS Biol 2024 Dec 20;22(12):e3002963
PMID:24763107 - Absolute proteome and phosphoproteome dynamics during the cell cycle of Schizosaccharomyces pombe (Fission Yeast).
Carpy A et al. Mol Cell Proteomics 2014 Aug;13(8):1925-36
PMID:39476757 - Characterization of Ksg1 protein kinase-dependent phosphoproteome in the fission yeast S. pombe.
Cipak L et al. Biochem Biophys Res Commun 2024 Oct 25;736:150895
PMID:31064814 - Proximity-dependent biotinylation mediated by TurboID to identify protein-protein interaction networks in yeast.
Larochelle M et al. J Cell Sci 2019 May 31;132(11)
PMID:10872838 - Identification of a 26S proteasome-associated UCH in fission yeast.
Li T et al. Biochem Biophys Res Commun 2000 May 27;272(1):270-5
PMID:25720772 - Quantitative phosphoproteomics reveals pathways for coordination of cell growth and division by the conserved fission yeast kinase pom1.
Kettenbach AN et al. Mol Cell Proteomics 2015 May;14(5):1275-87
PMID:21098295 - Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution.
Bohn S et al. Proc Natl Acad Sci U S A 2010 Dec 07;107(49):20992-7
PMID:39473973 - Limiting 20S proteasome assembly leads to unbalanced nucleo-cytoplasmic distribution of 26S/30S proteasomes and chronic proteotoxicity.
Ruiz-Romero G et al. iScience 2024 Nov 15;27(11):111095
PMID:21712547 - Mitotic substrates of the kinase aurora with roles in chromatin regulation identified through quantitative phosphoproteomics of fission yeast.
Koch A et al. Sci Signal 2011 Jun 28;4(179):rs6
PMID:15533439 - Uch2/Uch37 is the major deubiquitinating enzyme associated with the 26S proteasome in fission yeast.
Stone M et al. J Mol Biol 2004 Nov 26;344(3):697-706
PMID:21760946 - Identification of genes affecting the toxicity of anti-cancer drug bortezomib by genome-wide screening in S. pombe.
Takeda K et al. PLoS One 2011;6(7):e22021
PMID:16823372 - ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe.
Matsuyama A et al. Nat Biotechnol 2006 Jul;24(7):841-7
PMID:26771498 - A Proteome-wide Fission Yeast Interactome Reveals Network Evolution Principles from Yeasts to Human.
Vo TV et al. Cell 2016 Jan 14;164(1-2):310-323
PMID:23163955 - Analysis of stress-induced duplex destabilization (SIDD) properties of replication origins, genes and intergenes in the fission yeast, Schizosaccharomyces pombe.
Yadav MP et al. BMC Res Notes 2012 Nov 19;5:643
PMID:37787768 - Broad functional profiling of fission yeast proteins using phenomics and machine learning.
Rodríguez-López M et al. Elife 2023 Oct 03;12
PMID:28765280 - The exocyst subunit Sec3 is regulated by a protein quality control pathway.
Kampmeyer C et al. J Biol Chem 2017 Sep 15;292(37):15240-15253