RSU1

Ras suppressor protein 1 is a protein that in humans is encoded by the RSU1 gene.^[5][6]

RSU1
Identifiers
Aliases	RSU1, RSP-1, Ras suppressor protein 1
External IDs	OMIM: 179555; MGI: 103040; HomoloGene: 7521; GeneCards: RSU1; OMA:RSU1 - orthologs
Gene location (Human) Chr. Chromosome 10 (human)[1] Band 10p13 Start 16,590,611 bp[1] End 16,817,463 bp[1]
Gene location (Mouse) Chr. Chromosome 2 (mouse)[2] Band 2|2 A1 Start 13,081,632 bp[2] End 13,276,226 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in popliteal artery tibial arteries right coronary artery left coronary artery Descending thoracic aorta ascending aorta Achilles tendon monocyte saphenous vein stromal cell of endometrium Top expressed in genital tubercle granulocyte ascending aorta umbilical cord calvaria external carotid artery tail of embryo endothelial cell of lymphatic vessel left lung lobe right lung lobe More reference expression data BioGPS More reference expression data
Gene ontology Molecular function protein binding Cellular component cytosol extracellular exosome focal adhesion Biological process positive regulation of GTPase activity regulation of cell-substrate adhesion signal transduction positive regulation of cell-substrate adhesion Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 6251 20163 Ensembl ENSG00000148484 ENSMUSG00000026727 UniProt Q15404 Q01730 RefSeq (mRNA) NM_012425 NM_152724 NM_009105 RefSeq (protein) NP_036557 NP_689937 n/a Location (UCSC) Chr 10: 16.59 – 16.82 Mb Chr 2: 13.08 – 13.28 Mb PubMed search [3] [4]
Wikidata
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This gene encodes a protein that is involved in the Ras signal transduction pathway, growth inhibition, and nerve-growth factor induced differentiation processes, as determined in mouse and human cell line studies. In mouse, the encoded protein was initially isolated based on its ability to inhibit v-Ras transformation. Multiple alternatively spliced transcript variants for this gene have been reported; one of these variants was found only in glioma tumors.^[6] RSU-1 has also been seen to act as a structural protein in integrin-mediated focal-adhesion complexes. It bind strongly to the protein PINCH.