Q9ER71 · RHOJ_MOUSE

  • Protein
    Rho-related GTP-binding protein RhoJ
  • Gene
    Rhoj
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plasma membrane-associated small GTPase specifically involved in angiogenesis (By similarity).
Required for endothelial cell migration during vascular development via its interaction with GLUL (By similarity).
Elicits the formation of F-actin-rich structures, thereby regulating endothelial cell migration (PubMed:10967094).

Features

Showing features for binding site.

121420406080100120140160180200
TypeIDPosition(s)Description
Binding site31-36GTP (UniProtKB | ChEBI)
Binding site46-53GTP (UniProtKB | ChEBI)
Binding site75-79GTP (UniProtKB | ChEBI)
Binding site133-136GTP (UniProtKB | ChEBI)
Binding site177-178GTP (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 Componentplasma membrane
Molecular FunctionGTP binding
Molecular FunctionGTPase activity
Molecular Functionprotein kinase binding
Biological Processactin cytoskeleton organization
Biological Processactin filament organization
Biological Processangiogenesis
Biological ProcessCdc42 protein signal transduction
Biological Processendocytosis
Biological Processestablishment or maintenance of cell polarity
Biological Processpositive regulation of cell migration involved in sprouting angiogenesis
Biological Processregulation of cell shape
Biological Processregulation of endothelial cell migration
Biological Processregulation of sprouting angiogenesis
Biological Processretina vasculature morphogenesis in camera-type eye
Biological ProcessRho protein signal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Rho-related GTP-binding protein RhoJ
  • Alternative names
    • Tc10-like GTP-binding protein

Gene names

    • Name
      Rhoj
    • Synonyms
      Arhj, Rhoi
      , Rhot, Tc10l, Tcl

Organism names

  • Taxonomic identifier
  • Strains
    • C57BL/6J
    • NOD
    • FVB/N-3
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q9ER71
  • Secondary accessions
    • Q3TX76
    • Q920E4
    • Q9CQA7

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Lipid-anchor
Note: Localization to the plasma membrane is regulated by GLUL.

Keywords

PTM/Processing

Features

Showing features for chain, lipidation, modified residue, propeptide.

TypeIDPosition(s)Description
ChainPRO_00001988701-211
Lipidation3S-palmitoyl cysteine
Lipidation11S-palmitoyl cysteine
Modified residue211Cysteine methyl ester
Lipidation211S-farnesyl cysteine
PropeptidePRO_0000281221212-214Removed in mature form

Post-translational modification

Palmitoylated; regulates localization to the plasma membrane and may be mediated by GLUL.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Highly expressed in heart with moderate levels in lung and liver (PubMed:10967094).
Very low levels detected in brain, spleen, skeletal muscle, kidney and testis (PubMed:10967094).

Gene expression databases

Interaction

Subunit

Interacts with the CRIB domains of proteins such as Pak1 and Was/Wasp (PubMed:10967094).
Interacts with GLUL (By similarity).

Protein-protein interaction databases

Miscellaneous

Structure

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif50-58Effector region

Sequence similarities

Belongs to the small GTPase superfamily. Rho family.

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.

This entry describes 2 isoforms produced by Alternative splicing.

Q9ER71-1

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
    214
  • Mass (Da)
    23,766
  • Last updated
    2002-10-25 v2
  • Checksum
    A8070C73583A8AA3
MSCRERTDSSCGCNGHEENRILKCVVVGDGAVGKTCLLMSYANDAFPEEYVPTVFDHYAVTVTVGGKQHLLGLYDTAGQEDYNQLRPLSYPNTDVFLICFSVVNPASYHNVQEEWVPELKDCMPHVPYVLIGTQIDLRDDPKTLARLLYMKEKPLTYEHGVKLAKAIGAQCYLECSALTQKGLKAVFDEAILTIFHPKKKKKGCLGCHGCCAII

Q9ER71-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 3 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
D3YX61D3YX61_MOUSERhoj171
G3UZM2G3UZM2_MOUSERhoj96
F2Z463F2Z463_MOUSERhoj167

Features

Showing features for alternative sequence, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0057094-13in isoform 2
Sequence conflict166in Ref. 3; AAL09441

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ276568
EMBL· GenBank· DDBJ
CAC06700.1
EMBL· GenBank· DDBJ
mRNA
AB060651
EMBL· GenBank· DDBJ
BAB91069.1
EMBL· GenBank· DDBJ
mRNA
AF309564
EMBL· GenBank· DDBJ
AAL09441.1
EMBL· GenBank· DDBJ
mRNA
AK003482
EMBL· GenBank· DDBJ
BAB22812.1
EMBL· GenBank· DDBJ
mRNA
AK003490
EMBL· GenBank· DDBJ
BAB22818.1
EMBL· GenBank· DDBJ
mRNA
AK156619
EMBL· GenBank· DDBJ
BAE33778.1
EMBL· GenBank· DDBJ
mRNA
AK159385
EMBL· GenBank· DDBJ
BAE35040.1
EMBL· GenBank· DDBJ
mRNA
BC043719
EMBL· GenBank· DDBJ
AAH43719.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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