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O96612 · UBPB_DICDI

Function

function

Required for proper prespore cell patterning. Plays a role in stabilizing mkkA by preventing it from being targeted for degradation. ubcB and ubpB differentially control ubiquitination/deubiquitination and degradation of mkkA in a cell-type-specific and temporally regulated manner.

Catalytic activity

  • Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
    EC:3.4.19.12 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

145150100150200250300350400450
TypeIDPosition(s)Description
Active site399Nucleophile
Active site408Proton acceptor

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functioncysteine-type deubiquitinase activity
Biological Processprotein deubiquitination
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

Gene names

    • Name
      ubpB
    • ORF names
      DDB_G0275021

Organism names

Accessions

  • Primary accession
    O96612
  • Secondary accessions
    • Q554A4
    • Q869X4

Proteomes

Organism-specific databases

Phenotypes & Variants

Disruption phenotype

Null cells differentiate into prestalk cells preferentially. They develop precociously and exhibit abnormal cell-type patterning with an increase in the prestalk domain and reduction in the prespore domain in the slug, and spore domain in a fruiting body. Null cells do not form the normal spherical sori seen in mature wild-type fruiting bodies. Instead, the sori remain elongated, similar to those seen in wild-type fruiting bodies that are not fully mature. The upper and lower cups of the fruiting body, which are derived from prestalk cells and anterior-like cells, are enlarged. The spore-containing region is reduced. Null cells form fruiting bodies at approximately 17 hours and exhibit precocious expression of the spore marker. The expression levels of the prespore/spore markers are lower in null cells compared to wild-type cells, whereas expression of the prestalk/stalk marker is elevated slightly. The loss of gene function, might lead to increased mkkA ubiquitination and a more rapid turnover of mkkA. This should result in a reduced level of mkkA activity, producing the above mentioned mkkA null cell type phenotype.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003890211-451Ubiquitin hydrolase B

Proteomic databases

Expression

Developmental stage

Found at low levels in vegetative cells and at higher levels during aggregation and mound formation (4 and 8 hours of development).

Interaction

Subunit

Interacts with mkkA (via F-box/WD40 domains).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region.

Type
IDPosition(s)Description
Domain19-450USP
Region83-154Disordered

Sequence similarities

Belongs to the peptidase C19 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    451
  • Mass (Da)
    51,134
  • Last updated
    1999-05-01 v1
  • MD5 Checksum
    D5F71B2474A014E636470259EC962324
MKNIEEMPSKSQLVAHRSRGLINTSNTCFMNVILQSLTGCQLFLRVIKNLSDLEDLGKYPTLHSFNQFYTEYFSNPTSNILNNNSNSTTTTSSSSTTATTTSTSNNNKSQTPTSPIQQHHQSQTNGLSNQPSVATQSQQQQQPQPPINPKHFNDLVKSFNSKVSPVPQTTVSPHSMVQVSKKKLKLQLYNNSLPQTICQQDAQEFLVFLLDLIHEEFLTLIKDIDIPKEDDKSTPTSTSIVDDNWEVVGKKGKTAIITNSQQELPKTPISQIFSGVLRSSFNRTGSKESITVEPFYCLHLDIRPEEINSLEDALKFFMKPEIIEGYTCSTKKIEISASKSWSFESLPRILIVHFKRFAFESDTSKKLDKLIRFPTQLSLSTASNHQTQKKYSLFSVVSHHGRGLSQGHYTCDIYQPQQAQWIRYDDSTFTEVKEQDVLNREAYLLLYQLVN

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF093690
EMBL· GenBank· DDBJ
AAC97115.1
EMBL· GenBank· DDBJ
mRNA
AAFI02000013
EMBL· GenBank· DDBJ
EAL69791.1
EMBL· GenBank· DDBJ
Genomic DNA Different termination.

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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