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
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 3,247,428 bp[2] End 3,309,969 bp[2]
Gene ontology Molecular function • nucleotide binding • GDP binding • GTP binding • myosin V binding • GO:0001948 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 • cell 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: 3.25 – 3.31 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. 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 = Hormon- und Stoffwechselforschung = Hormones et Métabolisme. 30 (11): 656–62. doi:10.1055/s-2007-978953. PMID 9918381.
• 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. 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.