Q9CTN4 · RHBT3_MOUSE

  • Protein
    Rho-related BTB domain-containing protein 3
  • Gene
    Rhobtb3
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at transcript level
  • Annotation score
    4/5

Function

function

Rab9-regulated ATPase required for endosome to Golgi transport. Involved in transport vesicle docking at the Golgi complex, possibly by participating in release M6PRBP1/TIP47 from vesicles to permit their efficient docking and fusion at the Golgi. Specifically binds Rab9, but not other Rab proteins. Has low intrinsic ATPase activity due to autoinhibition, which is relieved by Rab9 (By similarity).

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
Cellular Componentcytosol
Cellular ComponentGolgi apparatus
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionGTPase activity
Molecular Functionsmall GTPase binding
Molecular Functionubiquitin protein ligase binding
Biological Processmale gonad development
Biological Processproteasome-mediated ubiquitin-dependent protein catabolic process
Biological Processregulation of proteolysis
Biological Processretrograde transport, endosome to Golgi

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rho-related BTB domain-containing protein 3
  • EC number

Gene names

    • Name
      Rhobtb3
    • Synonyms
      Kiaa0878

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9CTN4
  • Secondary accessions
    • Q05DP2
    • Q3UTS4
    • Q80X55
    • Q9CVT0

Proteomes

Organism-specific databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001989651-611

Proteomic databases

PTM databases

Expression

Gene expression databases

Interaction

Subunit

Interacts with RAB9A and RAB9B (at lower level compared to RAB9A-binding). Interacts with M6PRBP1/TIP47 (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-175Rho-like
Domain254-356BTB 1
Domain420-487BTB 2
Region420-611Interaction with Rab9

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    611
  • Mass (Da)
    69,208
  • Last updated
    2009-10-13 v3
  • Checksum
    F053962BD8CA1CDF
MSIHIVALGNEGDTFHQDNRPSGLIRTYLGRSPLVSGDESSLLLNAASTVARPVFTEYQASAFGNVKLVVHDCPVWDIFDSDWYTSRNLIGGADIIVIKYNVNDKFSFHEVKDNYIPVIKRASNSVPVIIAAVGTRQNEELPCTCPLCTSDRGSCVTTTEGIQLAKELGATYLELHSLDDFYIGKYFGGVLEYFMIQALNQKTSEKMKKRKMTSSFHGIRPPQLEQPEKMPVLKAEASHYHSDLNNLLLCCQCVDVVFYHPEVTGVVEAHKIVLCSVSHVFMLLFNVKSPADIQDSSIIRTTQDLFAINRDAVLPGASQEAPSNPPLPVIVKDALFCSCLSDILRFIYSGAFQWEELEEDVRRKLKDSGDVSDIIEKVKCILKTPGKINCLRNCKTYQARKPLWFYNTSLKFFLNKPMLADVVFEIQGATVPAHRAILVARCEVMAAMFNGNYMEAKSVLIPVYGVSKETFLSFLEYLYTDSCCPAGIFQAMCLLICAEMYQVSRLQHICELFIITQLQSMPSRELASMNLDIVDLLKKAKFHHSDCLSTWLLHFIATNYLIFSQKPEFQDLSVEERSFVEKHRWPSNMYLKQLAEYRKYIHSRKCRCLVM

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A1Y7VMM2A0A1Y7VMM2_MOUSERhobtb3100
A0A1Y7VJQ5A0A1Y7VJQ5_MOUSERhobtb388
Q8BV11Q8BV11_MOUSERhobtb3260

Sequence caution

The sequence AAH05664.1 differs from that shown. Reason: Miscellaneous discrepancy Contaminating sequence. Potential poly-A sequence.
The sequence BAC98044.1 differs from that shown. Reason: Erroneous initiation

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict588in Ref. 3; BAB24689

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK129234
EMBL· GenBank· DDBJ
BAC98044.1
EMBL· GenBank· DDBJ
mRNA Different initiation
AK020938
EMBL· GenBank· DDBJ
-mRNA No translation available.
AK006650
EMBL· GenBank· DDBJ
BAB24689.1
EMBL· GenBank· DDBJ
mRNA
AK139158
EMBL· GenBank· DDBJ
BAE23906.1
EMBL· GenBank· DDBJ
mRNA
CH466563
EMBL· GenBank· DDBJ
EDL37111.1
EMBL· GenBank· DDBJ
Genomic DNA
BC005664
EMBL· GenBank· DDBJ
AAH05664.1
EMBL· GenBank· DDBJ
mRNA Sequence problems.
BC050836
EMBL· GenBank· DDBJ
AAH50836.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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