RAB10

Ras-related protein Rab-10 is a protein that in humans is encoded by the RAB10 gene.^[5][6]

RAB10
Identifiers
Aliases	RAB10, member RAS oncogene family
External IDs	OMIM: 612672; MGI: 105066; HomoloGene: 41111; GeneCards: RAB10; OMA:RAB10 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p23.3 Start 26,034,084 bp[1] End 26,137,454 bp[1]
Gene location (Mouse) Chr. Chromosome 12 (mouse)[2] Band 12 A1.1|12 1.71 cM Start 3,297,428 bp[2] End 3,359,969 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in pancreatic epithelial cell mucosa of ileum pancreatic ductal cell endothelial cell tibialis anterior muscle gingival epithelium vastus lateralis muscle deltoid muscle mucosa of pharynx oral cavity Top expressed in vastus lateralis muscle ascending aorta muscle of thigh aortic valve knee joint dorsomedial hypothalamic nucleus skin of external ear ventral tegmental area median eminence medial head of gastrocnemius muscle More reference expression data BioGPS n/a
Gene ontology Molecular function nucleotide binding GDP binding GTP binding myosin V binding protein binding cadherin binding involved in cell-cell adhesion GTPase activity Cellular component recycling endosome endosome phagocytic vesicle membrane Golgi apparatus cell projection endoplasmic reticulum membrane membrane focal adhesion insulin-responsive compartment Golgi membrane endoplasmic reticulum tubular network recycling endosome membrane exocyst endoplasmic reticulum endosome membrane extracellular exosome cytoplasmic vesicle membrane cytoplasmic vesicle trans-Golgi network cytosol plasma membrane cilium secretory granule membrane exocytic vesicle cytoplasm synaptic vesicle perinuclear region of cytoplasm Biological process endoplasmic reticulum tubular network organization polarized epithelial cell differentiation antigen processing and presentation establishment of neuroblast polarity axonogenesis establishment of protein localization to membrane endosomal transport cellular response to insulin stimulus protein transport establishment of protein localization to endoplasmic reticulum membrane protein localization to plasma membrane Golgi to plasma membrane transport vesicle-mediated transport Golgi to plasma membrane protein transport cell-cell adhesion neutrophil degranulation vesicle docking involved in exocytosis protein secretion regulation of exocytosis transport protein localization to basolateral plasma membrane intracellular protein transport Rab protein signal transduction Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10890 19325 Ensembl ENSG00000084733 ENSMUSG00000020671 UniProt P61026 P61027 RefSeq (mRNA) NM_016131 NM_016676 RefSeq (protein) NP_057215 NP_057885 Location (UCSC) Chr 2: 26.03 – 26.14 Mb Chr 12: 3.3 – 3.36 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Interactions

RAB10 has been shown to interact with AP1S1.^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000084733 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000020671 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Chen YT, Holcomb C, Moore HP (Jul 1993). "Expression and localization of two low molecular weight GTP-binding proteins, Rab8 and Rab10, by epitope tag". Proceedings of the National Academy of Sciences of the United States of America. 90 (14): 6508–12. Bibcode:1993PNAS...90.6508C. doi:10.1073/pnas.90.14.6508. PMC 46961. PMID 7688123.
6. "Entrez Gene: RAB10 RAB10, member RAS oncogene family".
7. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.

Further reading

• Bao S, Zhu J, Garvey WT (Nov 1998). "Cloning of Rab GTPases expressed in human skeletal muscle: studies in insulin-resistant subjects". Hormone and Metabolic Research. 30 (11): 656–62. doi:10.1055/s-2007-978953. PMID 9918381. S2CID 23540699.
• Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL (Aug 2000). "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning". Proceedings of the National Academy of Sciences of the United States of America. 97 (17): 9543–8. Bibcode:2000PNAS...97.9543H. doi:10.1073/pnas.160270997. PMC 16901. PMID 10931946.
• Fukuda M (Apr 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
• Sonkoly E, Bata-Csorgo Z, Pivarcsi A, Polyanka H, Kenderessy-Szabo A, Molnar G, Szentpali K, Bari L, Megyeri K, Mandi Y, Dobozy A, Kemeny L, Szell M (Jun 2005). "Identification and characterization of a novel, psoriasis susceptibility-related noncoding RNA gene, PRINS". The Journal of Biological Chemistry. 280 (25): 24159–67. doi:10.1074/jbc.M501704200. PMID 15855153.
• Larance M, Ramm G, Stöckli J, van Dam EM, Winata S, Wasinger V, Simpson F, Graham M, Junutula JR, Guilhaus M, James DE (Nov 2005). "Characterization of the role of the Rab GTPase-activating protein AS160 in insulin-regulated GLUT4 trafficking". The Journal of Biological Chemistry. 280 (45): 37803–13. doi:10.1074/jbc.M503897200. PMID 16154996.