A0A5N4E6H8 · A0A5N4E6H8_CAMDR

Function

function

Deubiquitinating enzyme that removes conjugated ubiquitin from specific proteins to regulate different cellular processes.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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)

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 Processcell division
Biological Processprotein deubiquitination
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Ubiquitin carboxyl-terminal hydrolase
  • EC number

Gene names

    • ORF names
      Cadr_000007354

Organism names

  • Taxonomic identifier
  • Strain
    • Drom800
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Tylopoda > Camelidae > Camelus

Accessions

  • Primary accession
    A0A5N4E6H8

Proteomes

PTM/Processing

Features

Showing features for signal, chain.

TypeIDPosition(s)Description
Signal1-15
ChainPRO_502443606816-981Ubiquitin carboxyl-terminal hydrolase

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region134-328Disordered
Compositional bias143-169Polar residues
Compositional bias197-221Polar residues
Compositional bias222-248Basic and acidic residues
Compositional bias249-325Polar residues
Domain365-953USP
Region721-833Disordered
Compositional bias722-739Basic and acidic residues
Compositional bias774-791Basic and acidic residues

Sequence similarities

Belongs to the peptidase C19 family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    981
  • Mass (Da)
    110,680
  • Last updated
    2020-02-26 v1
  • Checksum
    B90086FF065659FD
MEFLVFLISMPLVAAKQFIFKESMPPLKIHGPIRIRSMQTGITKWKEGSFEIVEKENKVSLVVHYNTGGIPRIFQLSHNIKNVVLRPSGAKQSRLMLTLQDNSFLSIDKVPSKDAEEMRLFLDAVHQNRLNAAMKPQGSGSFGAILGSRTSQKETNRQLSYSDNQVSSKRGSLETKDDIPFRKVLSNPGRGSIKTAAGSGITATRTIPSLTSTSTPLRSGLLENRTEKRKRMLSSGSELNEDYPKENDSSSNNKAMTDPSRKYLTSSREKQLSLKQSEENRTSGLLPLQSSSFYGSRAASKDYSPGNTNLDRTNISSQTPSAKRSLGFLPQPAPLSVKKLRCNQDYTGWNKPRVPLSSHQQQQLQGFSNLGNTCYMNAILQSLFSLQSFANDLLKQGIPWKKIPLNALIRRFAHLLVKKDICNSETKKDLLKKVKNAISATAERFSGYMQNDAHEFLSQCLDQLKEDMEKLNKTWKTEPVPGEENSPDISATRVYTCPVITNLEFEVQHSIICKACGETIPKREQFNDLSIDLPRRKKPLPPRSIQDSLDLFFRAEELEYSCEKCGGKCALVRHKFNRLPRILILHLKRYSFNVALSLNNKIGQQVIIPRYLTLSSHCTENTKPPFNLGWSAQMAMNFTFKSKSSVALCLDSDSEDELKRSVALSQRLCEISGSEQQQEDLEKDSKLCRIEPDKSELENSGFDGMSEEELLAAVLEISKREASPSLSHEDDDKPTSSPDTGFADDDIQEIPENPDSMETEKPKTVTEPDPASFTEITKDCDENKENKTPEGSQGEVDWLQQYDMEREREEQELQQALAQSLQEQEAWEQKEDDDLKRATELSLQEFNNSFLDSLGSDEDSGNEDVLDMEYTEAEAEELKRNAETGNLPHSYRLISVVSHIGSTSSSGHYISDVYDIKKQAWFTYNDLEVSKIQEASVQSDRDRSGYIFFYMHKEIFDELLETEKNSQALSMEVGKTTRQAS

Computationally mapped potential isoform sequences

There are 4 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A5N4E6V6A0A5N4E6V6_CAMDRCadr_0000073541083
A0A5N4E7T9A0A5N4E7T9_CAMDRCadr_000007354412
A0A5N4E7G9A0A5N4E7G9_CAMDRCadr_0000073541003
A0A5N4E702A0A5N4E702_CAMDRCadr_000007354620

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias143-169Polar residues
Compositional bias197-221Polar residues
Compositional bias222-248Basic and acidic residues
Compositional bias249-325Polar residues
Compositional bias722-739Basic and acidic residues
Compositional bias774-791Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JWIN03000005
EMBL· GenBank· DDBJ
KAB1279098.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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