A0AAD8YSG1 · A0AAD8YSG1_9TELE

  • Protein
    SH3 domain-binding protein 5
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

Function

function

Catalytic release of biotin from biocytin, the product of biotin-dependent carboxylases degradation.
Functions as guanine nucleotide exchange factor (GEF) for RAB11A.

Caution

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

Catalytic activity

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 Componentcytoplasm
Molecular Functionguanyl-nucleotide exchange factor activity
Molecular Functionhydrolase activity
Molecular FunctionSH3 domain binding
Biological Processintracellular signal transduction

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    SH3 domain-binding protein 5
  • Short names
    SH3BP-5

Gene names

    • ORF names
      P4O66_018871

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CB-2022
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Gymnotiformes > Gymnotoidei > Gymnotidae > Electrophorus

Accessions

  • Primary accession
    A0AAD8YSG1

Proteomes

Subcellular Location

Cytoplasm
Note: Colocalizes with RAB11A on cytoplasmic vesicle membranes.

Keywords

Interaction

Subunit

Interacts with GDP-bound and nucleotide-free forms of RAB11A.

Family & Domains

Features

Showing features for region, coiled coil, compositional bias, domain.

TypeIDPosition(s)Description
Region1-41Disordered
Coiled coil89-130
Coiled coil168-223
Compositional bias283-338Polar residues
Region283-351Disordered
Domain420-671CN hydrolase
Region909-946Disordered
Compositional bias916-935Basic and acidic residues

Domain

The N-terminal half of the protein mediates interaction with RAB11A and functions as guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape.

Sequence similarities

Belongs to the SH3BP5 family.
Belongs to the carbon-nitrogen hydrolase superfamily. BTD/VNN family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    946
  • Mass (Da)
    104,771
  • Last updated
    2024-05-29 v1
  • Checksum
    B01B85E0996B26BD
MDDSVKGNKSDGETESPEDEEVDPRIQGELEKLNQSTDDINRWESDLEDSRKRFRAVLVEATLKLDEQVKKIGKAVEDSKPYWEARKVARQAQVEAQRATQEFQRAIEILRAAKETIALAEERLLEEDSRQFDSAWQEMLNHATQRVMEAEQSRTHSELEHKETAARYTAAVNHVRQLEKKLKRAVNKSRPYFELKAKYYLQLEQLKRRVDECQAKLTQAKADYRSALCTLEAISDEIHTRRRLTAMGPRICGVGAERDMMDGDIANFKTESDGISVMSETFEESCNGVTSEEDPEMQSTCSLSSNSTPVNLPRPYLATPSSPYPSSSSSSSSTTPSPRPSDPELPSPDSLECLDLASATLGPRSECSGASSPECERERGSSALCSLACSVAGQLALARSVSISQHPGGLMASYGLTAAILGACVLAIHLIGAEETLYVAAVYEHRVILNPRSGVPLRRRAALEHMEKNLHAFAEQAALAALQVLRRLSCMARKNRLFLVANMPDRQPCSRASDPLCPPDGQYQFNTDVVFSDNGTLVARYHKQNLYFEAAFDTPLRNKYVTFTTPFAGRFGVFTCFDILFREPAVTLVRDMGVRQLVYPTAWMNQLPLLAAVQFQRSFSYSAGVTLLAANVRAAALGMTGSGIFTPWEAVYHHDSTEGEQGRLLVSRVPVLDPLAVVGRARPSLVPFSGHPKAEGAVEEDETWPDCNNLQADTRRRKPEATFCLKEESGYREELLAEEPTPPFTSTMMYDNFTLVLLQGREGNLTACDGSFCCHLLFRRSDPPEEELYALGAFDGLHVVHGTYYLEVCALVKCPGQHKGSCGGETERAQTLIDFQLDGIFSTEHVYAGVLGSGMTLDRPDQSGWQSGGRFYMKRRGMTTGLVTAVLYGRVYEKDSCFLKVPETLAPQAGEGGEELGVVTDKRGGHNDASRGRYSLKDRSTQNPLF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias283-338Polar residues
Compositional bias916-935Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAROKS010000026
EMBL· GenBank· DDBJ
KAK1785504.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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