Q9BYZ6 · RHBT2_HUMAN

  • Protein
    Rho-related BTB domain-containing protein 2
  • Gene
    RHOBTB2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

Features

Showing features for binding site.

1727100200300400500600700
TypeIDPosition(s)Description
Binding site21-28GTP (UniProtKB | ChEBI)
Binding site84-88GTP (UniProtKB | ChEBI)
Binding site140-143GTP (UniProtKB | ChEBI)

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 Componentendosome membrane
Cellular Componentplasma membrane
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionprotein kinase binding
Biological Processactin filament organization
Biological ProcessCdc42 protein signal transduction
Biological Processendocytosis
Biological Processestablishment or maintenance of cell polarity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rho-related BTB domain-containing protein 2
  • Alternative names
    • Deleted in breast cancer 2 gene protein
    • p83

Gene names

    • Name
      RHOBTB2
    • Synonyms
      DBC2, KIAA0717

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9BYZ6
  • Secondary accessions
    • A8K9Z8
    • D3DSR8
    • E9PBU2
    • E9PEI7
    • O94825

Proteomes

Organism-specific databases

Subcellular Location

Disease & Variants

Involvement in disease

Developmental and epileptic encephalopathy 64 (DEE64)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    A form of epileptic encephalopathy, a heterogeneous group of severe early-onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent. DEE64 is an autosomal dominant form characterized by onset of seizures usually in the first year of life. Seizure types are variable and include focal dyscognitive and generalized tonic-clonic seizures, as well as febrile seizures in the mildest affected individuals. Seizures tend to respond to medical treatment.
  • See also
    MIM:618004
Natural variants in DEE64
Variant IDPosition(s)ChangeDescription
VAR_080812452A>Gin DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504656
VAR_080813461R>Hin DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504663
VAR_080814485R>Cin DEE64; decreased proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1563292586
VAR_079030488N>Din DEE64; also found in a patient with Rett syndrome-like phenotype; dbSNP:rs1554504678
VAR_080815489R>Qin DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504684
VAR_080816489R>Win DEE64; dbSNP:rs1554504681

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis284Results in decreased interaction with CUL3.
Natural variantVAR_080812452in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504656
Natural variantVAR_080813461in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504663
Natural variantVAR_080814485in DEE64; decreased proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1563292586
Natural variantVAR_079030488in DEE64; also found in a patient with Rett syndrome-like phenotype; dbSNP:rs1554504678
Natural variantVAR_080815489in DEE64; reduced RHOBTB2 proteasomal degradation; does not affect interaction with CUL3; dbSNP:rs1554504684
Natural variantVAR_080816489in DEE64; dbSNP:rs1554504681

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 835 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001989621-727

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitous, with highest levels in neural tissues. Expression is also detected in fetal lung, heart, and brain.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with HSP90AA1 and HSP90AB1 (PubMed:26517842).
Interacts with CUL3 (PubMed:29276004).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for region, domain.

TypeIDPosition(s)Description
Region1-210Rho-like
Domain266-442BTB 1
Region304-333Disordered
Domain500-567BTB 2
Region703-727Disordered

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q9BYZ6-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    727
  • Mass (Da)
    82,626
  • Last updated
    2002-11-28 v2
  • Checksum
    25C7493B2894A1B3
MDSDMDYERPNVETIKCVVVGDNAVGKTRLICARACNATLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDDVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLHHVKTMWYPEIKHFCPRAPVILVGCQLDLRYADLEAVNRARRPLARPIKPNEILPPEKGREVAKELGIPYYETSVVAQFGIKDVFDNAIRAALISRRHLQFWKSHLRNVQRPLLQAPFLPPKPPPPIIVVPDPPSSSEECPAHLLEDPLCADVILVLQERVRIFAHKIYLSTSSSKFYDLFLMDLSEGELGGPSEPGGTHPEDHQGHSDQHHHHHHHHHGRDFLLRAASFDVCESVDEAGGSGPAGLRASTSDGILRGNGTGYLPGRGRVLSSWSRAFVSIQEEMAEDPLTYKSRLMVVVKMDSSIQPGPFRAVLKYLYTGELDENERDLMHIAHIAELLEVFDLRMMVANILNNEAFMNQEITKAFHVRRTNRVKECLAKGTFSDVTFILDDGTISAHKPLLISSCDWMAAMFGGPFVESSTREVVFPYTSKSCMRAVLEYLYTGMFTSSPDLDDMKLIILANRLCLPHLVALTEQYTVTGLMEATQMMVDIDGDVLVFLELAQFHCAYQLADWCLHHICTNYNNVCRKFPRDMKAMSPENQEYFEKHRWPPVWYLKEEDHYQRARKEREKEDYLHLKRQPKRRWLFWNSPSSPSSSAASSSSPSSSSAVV

Q9BYZ6-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MQAWRKGPDGPQKTSSDSMSRLM

Q9BYZ6-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-1: M → MKARSRLM

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
A0A8I5KV41A0A8I5KV41_HUMANRHOBTB2736
E5RI44E5RI44_HUMANRHOBTB2182

Sequence caution

The sequence AAH34917.1 differs from that shown. Reason: Erroneous initiation Truncated N-terminus.
The sequence BAA34437.2 differs from that shown. Reason: Erroneous initiation Extended N-terminus.

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0540981in isoform 2
Alternative sequenceVSP_0540991in isoform 3
Sequence conflict255in Ref. 2; AAG61157
Sequence conflict269in Ref. 6; BAF85552

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY009093
EMBL· GenBank· DDBJ
AAG61157.1
EMBL· GenBank· DDBJ
mRNA
AF315385
EMBL· GenBank· DDBJ
AAK07562.1
EMBL· GenBank· DDBJ
Genomic DNA
AB018260
EMBL· GenBank· DDBJ
BAA34437.2
EMBL· GenBank· DDBJ
mRNA Different initiation
AK292863
EMBL· GenBank· DDBJ
BAF85552.1
EMBL· GenBank· DDBJ
mRNA
AC107959
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471080
EMBL· GenBank· DDBJ
EAW63644.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471080
EMBL· GenBank· DDBJ
EAW63646.1
EMBL· GenBank· DDBJ
Genomic DNA
BC034917
EMBL· GenBank· DDBJ
AAH34917.1
EMBL· GenBank· DDBJ
mRNA Different initiation

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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp