Rho-related GTP-binding protein RhoG (RHOG)

The protein contains 191 amino acids for an estimated molecular weight of 21309 Da.

 

Required for the formation of membrane ruffles during macropinocytosis. Plays a role in cell migration and is required for the formation of cup-like structures during trans-endothelial migration of leukocytes. In case of Salmonella enterica infection, activated by SopB and ARHGEF26/SGEF, which induces cytoskeleton rearrangements and promotes bacterial entry. (updated: March 4, 2015)

Protein identification was indicated in the following studies:

  1. Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
  2. Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
  3. Wilson and co-workers. (2016) Comparison of the Proteome of Adult and Cord Erythroid Cells, and Changes in the Proteome Following Reticulocyte Maturation. Mol Cell Proteomics. 15(6), 1938-1946.
  4. Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
  5. D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
  6. Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.

Methods

The following articles were analysed to gather the proteome content of erythrocytes.

The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.

PublicationIdentification 1Uniprot mapping 2Not mapped /
Obsolete		TrEMBLSwiss-Prot
Goodman (2013)2289 (gene list)227853205992269
Lange (2014)123412347281224
Hegedus (2015)2638262202352387
Wilson (2016)165815281702911068
d'Alessandro (2017)18261817201815
Bryk (2017)20902060101081942
Chu (2018)18531804553621387

1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry

The compilation of older studies can be retrieved from the Red Blood Cell Collection database.

The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.

No sequence conservation computed yet.
Protein sequence (FASTA)
Protein coevolution profile (FreeContact)
Multiple Sequence Alignment (Muscle)

This protein is annotated as membranous in Gene Ontology, is annotated as membranous in UniProt.


Interpro domains
Total structural coverage: 100%
Model score: 0
No model available.

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The reference OMIM entry for this protein is 179505

Ras homolog gene family, member g; rhog
Ras homolog gene g
Arhg

DESCRIPTION

ARHG is a member of the RAS superfamily of genes, which encode GTP-binding proteins that act in the pathway of signal transduction and play a key role in the regulation of cellular functions.

CLONING

Vincent et al. (1992) isolated a new member of the RAS homolog gene family, ARHG, from hamster and human. The ARHG gene is a late induced gene, and RNA accumulation is proportional to the strength of the mitogen used. Phylogenetic studies suggested that it may have diverged early during evolution.

GENE FUNCTION

Katoh and Negishi (2003) demonstrated that RHO G interacts directly with ELMO2 (606421) in a GTP-dependent manner and forms a ternary complex with DOCK180 (601403) to induce activation of RAC1 (602048). The RHO G-ELMO2-DOCK180 pathway is required for activation of RAC1 and cell spreading mediated by integrin, as well as for neurite outgrowth induced by nerve growth factor. Katoh and Negishi (2003) concluded that RHO G activates RAC1 through ELMO and DOCK180 to control cell morphology.

GENE STRUCTURE

Le Gallic and Fort (1997) determined that the ARHG gene spans 25 kb and contains only 2 exons with an intervening 20-kb intron. The first exon is noncoding and 85% GC-rich. The ARHG gene lacks TATA and CAAT boxes, typical of housekeeping genes.

MAPPING

By fluorescence in situ hybridization on human metaphase chromosomes, Taviaux et al. (1993) assigned the RHOG gene to 11p15.5-p.15.4. Precise observations indicated it was located distal to WEE1 (193525). ... More on the omim web site

Subscribe to this protein entry history

Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated

Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated

March 16, 2016: Protein entry updated
Automatic update: OMIM entry 179505 was added.