A0A2J7RL21 · A0A2J7RL21_9NEOP

Function

function

E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome.

Caution

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

Catalytic activity

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N6-ubiquitinyl-[acceptor protein]-L-lysine.
    EC:2.3.2.27 (UniProtKB | ENZYME | Rhea)

Pathway

Protein modification; protein ubiquitination.

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
Cellular Componentmembrane raft
Cellular Componentplasma membrane
Molecular Functioncalcium ion binding
Molecular Functionphosphotyrosine residue binding
Molecular Functionreceptor tyrosine kinase binding
Molecular FunctionSH3 domain binding
Molecular Functionubiquitin protein ligase activity
Biological Processnegative regulation of epidermal growth factor-activated receptor activity
Biological Processprotein ubiquitination
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    E3 ubiquitin-protein ligase CBL
  • EC number

Gene names

    • ORF names
      B7P43_G12308

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Polyneoptera > Dictyoptera > Blattodea > Blattoidea > Termitoidae > Kalotermitidae > Cryptotermitinae > Cryptotermes

Accessions

  • Primary accession
    A0A2J7RL21

Proteomes

Subcellular Location

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain1-130Cbl-PTB
Domain160-199RING-type
Region253-320Disordered
Compositional bias282-297Pro residues
Compositional bias298-313Polar residues
Compositional bias357-394Polar residues
Region357-462Disordered
Compositional bias395-411Pro residues
Compositional bias412-462Polar residues

Domain

The N-terminus is composed of the phosphotyrosine binding (PTB) domain, a short linker region and the RING-type zinc finger. The PTB domain, which is also called TKB (tyrosine kinase binding) domain, is composed of three different subdomains: a four-helix bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    524
  • Mass (Da)
    56,707
  • Last updated
    2018-03-28 v1
  • Checksum
    3CC148EBEC9C290F
MALKSTIDLTCNDYISNFEFDVFTRLFQPWTTLLRNWQILAVTHPGYVAFLTYDEVKARLQKYITKPGSYVFRLSCTRLGQWAIGYVTADGEILQTIPQNKSLCQALLDGYREGFYLFPDGRNVNPDLSWAVQPTPEDHIKVTQEQYELYCEMGSTFQLCKICAENDKDIRIEPCGHLLCTPCLTSWQDSEGQGCPFCRAEIKGTEQIVVDPFDPKRQHKAGSTGNLVDLDEDEEDLSNWNCNISSLQALALSPRSETGDGRGGRSPMISPRASPQLLRRGTTPVAPPPPLPPRRASPTLGSPTSSPSNQLTVPKEDAPPPPCTCTVMIVAQETEEPETLSGIADTRYDILQTSGSSMANSSSKVAGTSSHVRHQSCPALPSSCSTTMLPSKSNTTPLFPPPLPPPTVPSIPSTSLTSSVSTSQSSNALSASVASTSATSPRQPTSTESSSGNSLQRQHSGGNAHTIHYAELADISEEPSYENTIIIPGGTSLIKPVYSAAVETDVPNSAVIAQNIKPLTLEAR

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
A0A2J7RL16A0A2J7RL16_9NEOPB7P43_G12308241

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias282-297Pro residues
Compositional bias298-313Polar residues
Compositional bias357-394Polar residues
Compositional bias395-411Pro residues
Compositional bias412-462Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NEVH01002700
EMBL· GenBank· DDBJ
PNF41533.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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