RAB8A

Protein-coding gene in the species Homo sapiens
RAB8A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3QBT, 3TNF, 4LHV, 4LHW, 4LHX, 4LHY, 4LHZ, 4LI0

Identifiers
AliasesRAB8A, MEL, RAB8, member RAS oncogene family
External IDsOMIM: 165040; MGI: 96960; HomoloGene: 100934; GeneCards: RAB8A; OMA:RAB8A - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for RAB8A
Genomic location for RAB8A
Band19p13.11Start16,111,889 bp[1]
End16,134,234 bp[1]
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)[2]
Chromosome 8 (mouse)
Genomic location for RAB8A
Genomic location for RAB8A
Band8 B3.3|8 34.84 cMStart72,915,044 bp[2]
End72,937,748 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • monocyte

  • mucosa of ileum

  • bone marrow cells

  • duodenum

  • mucosa of sigmoid colon

  • jejunal mucosa

  • blood

  • epithelium of colon

  • granulocyte

  • human penis
Top expressed in
  • granulocyte

  • molar

  • yolk sac

  • tibiofemoral joint

  • thymus

  • duodenum

  • right kidney

  • epithelium of small intestine

  • ventricular zone

  • medial ganglionic eminence
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GDP binding
  • GTP binding
  • myosin V binding
  • protein binding
  • protein kinase binding
  • GTPase activity
Cellular component
  • cytoplasm
  • ciliary basal body
  • recycling endosome
  • cytosol
  • endosome
  • centrosome
  • phagocytic vesicle membrane
  • Golgi apparatus
  • cell projection
  • membrane
  • postsynaptic density
  • synaptic vesicle
  • Golgi membrane
  • cilium
  • ciliary base
  • neuronal cell body
  • dendrite
  • phagocytic vesicle
  • centriole
  • extracellular exosome
  • cytoskeleton
  • cytoplasmic vesicle
  • extracellular matrix
  • plasma membrane
  • trans-Golgi network transport vesicle
  • trans-Golgi network membrane
  • dendritic spine
  • recycling endosome membrane
  • non-motile cilium
  • secretory granule membrane
  • midbody
  • synapse
  • glutamatergic synapse
Biological process
  • regulation of long-term neuronal synaptic plasticity
  • regulation of protein transport
  • axonogenesis
  • vesicle docking involved in exocytosis
  • protein secretion
  • regulation of protein localization
  • cell projection organization
  • G2/M transition of mitotic cell cycle
  • Golgi vesicle fusion to target membrane
  • protein transport
  • protein localization to plasma membrane
  • cellular response to insulin stimulus
  • cilium assembly
  • ciliary basal body-plasma membrane docking
  • neurotransmitter receptor transport to postsynaptic membrane
  • regulation of autophagy
  • autophagy
  • post-translational protein modification
  • regulation of exocytosis
  • transport
  • intracellular protein transport
  • Rab protein signal transduction
  • neurotransmitter receptor transport, endosome to postsynaptic membrane
  • vesicle-mediated transport in synapse
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

4218

17274

Ensembl

ENSG00000167461

ENSMUSG00000003037

UniProt

P61006

P55258

RefSeq (mRNA)

NM_005370

NM_023126

RefSeq (protein)

NP_005361
NP_005361.2

NP_075615

Location (UCSC)Chr 19: 16.11 – 16.13 MbChr 8: 72.92 – 72.94 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras-related protein Rab-8A is a protein that in humans is encoded by the RAB8A gene.[5][6][7]

Function

The protein encoded by this gene is a member of the RAS superfamily which are small GTP/GDP-binding proteins with an average size of 200 amino acids. The RAS-related proteins of the RAB/YPT family may play a role in the transport of proteins from the endoplasmic reticulum to the Golgi and the plasma membrane. This protein shares 97%, 96%, and 51% similarity with the dog RAB8, mouse MEL, and mouse YPT1 proteins, respectively and contains the 4 GTP/GDP-binding sites that are present in all the RAS proteins. The putative effector-binding site of this protein is similar to that of the RAB/YPT proteins. However, this protein contains a C-terminal CAAX motif that is characteristic of many RAS superfamily members but which is not found in YPT1 and the majority of RAB proteins. Although this gene was isolated as a transforming gene from a melanoma cell line, no linkage between MEL and malignant melanoma has been demonstrated. This oncogene is located 800 kb distal to MY09B on chromosome 19p13.1.[7]

Interactions

RAB8A has been shown to interact with Optineurin[8] and MAP4K2.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000167461 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003037 – 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. ^ Nimmo ER, Sanders PG, Padua RA, Hughes D, Williamson R, Johnson KJ (Aug 1991). "The MEL gene: a new member of the RAB/YPT class of RAS-related genes". Oncogene. 6 (8): 1347–51. PMID 1886711.
  6. ^ Huber LA, Pimplikar S, Parton RG, Virta H, Zerial M, Simons K (Oct 1993). "Rab8, a small GTPase involved in vesicular traffic between the TGN and the basolateral plasma membrane". The Journal of Cell Biology. 123 (1): 35–45. doi:10.1083/jcb.123.1.35. PMC 2119815. PMID 8408203.
  7. ^ a b "Entrez Gene: RAB8A RAB8A, member RAS oncogene family".
  8. ^ Hattula K, Peränen J (2000). "FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis". Current Biology. 10 (24): 1603–6. Bibcode:2000CBio...10.1603H. doi:10.1016/S0960-9822(00)00864-2. PMID 11137014. S2CID 12836037.
  9. ^ Ren M, Zeng J, De Lemos-Chiarandini C, Rosenfeld M, Adesnik M, Sabatini DD (May 1996). "In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 5151–5. Bibcode:1996PNAS...93.5151R. doi:10.1073/pnas.93.10.5151. PMC 39423. PMID 8643544.

Further reading

  • Newport J, Roemer MI (Mar 1975). "Comparative perinatal mortality under medical care foundations and other delivery models". Inquiry. 12 (1): 10–7. PMID 123217.
  • Nimmo E, Padua RA, Hughes D, Brook JD, Williamson R, Johnson KJ (Mar 1989). "Confirmation and refinement of the localisation of the c-MEL locus on chromosome 19 by physical and genetic mapping". Human Genetics. 81 (4): 382–4. doi:10.1007/BF00283697. PMID 2564840. S2CID 25002878.
  • Zahraoui A, Joberty G, Arpin M, Fontaine JJ, Hellio R, Tavitian A, Louvard D (Jan 1994). "A small rab GTPase is distributed in cytoplasmic vesicles in non polarized cells but colocalizes with the tight junction marker ZO-1 in polarized epithelial cells". The Journal of Cell Biology. 124 (1–2): 101–15. doi:10.1083/jcb.124.1.101. PMC 2119893. PMID 8294494.
  • Joberty G, Tavitian A, Zahraoui A (Sep 1993). "Isoprenylation of Rab proteins possessing a C-terminal CaaX motif". FEBS Letters. 330 (3): 323–8. doi:10.1016/0014-5793(93)80897-4. PMID 8375503. S2CID 29047580.
  • Ren M, Zeng J, De Lemos-Chiarandini C, Rosenfeld M, Adesnik M, Sabatini DD (May 1996). "In its active form, the GTP-binding protein rab8 interacts with a stress-activated protein kinase". Proceedings of the National Academy of Sciences of the United States of America. 93 (10): 5151–5. Bibcode:1996PNAS...93.5151R. doi:10.1073/pnas.93.10.5151. PMC 39423. PMID 8643544.
  • Bähler M, Kehrer I, Gordon L, Stoffler HE, Olsen AS (Jul 1997). "Physical mapping of human myosin-IXB (MYO9B), the human orthologue of the rat myosin myr 5, to chromosome 19p13.1". Genomics. 43 (1): 107–9. doi:10.1006/geno.1997.4776. PMID 9226381.
  • Wilson AL, Erdman RA, Castellano F, Maltese WA (Aug 1998). "Prenylation of Rab8 GTPase by type I and type II geranylgeranyl transferases". The Biochemical Journal. 333 (Pt 3): 497–504. doi:10.1042/bj3330497. PMC 1219609. PMID 9677305.
  • 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.
  • Shisheva A, Chinni SR, DeMarco C (Sep 1999). "General role of GDP dissociation inhibitor 2 in membrane release of Rab proteins: modulations of its functional interactions by in vitro and in vivo structural modifications". Biochemistry. 38 (36): 11711–21. doi:10.1021/bi990200r. PMID 10512627.
  • Hattula K, Peränen J (2001). "FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis". Current Biology. 10 (24): 1603–6. Bibcode:2000CBio...10.1603H. doi:10.1016/S0960-9822(00)00864-2. PMID 11137014. S2CID 12836037.
  • Kuroda TS, Fukuda M, Ariga H, Mikoshiba K (Mar 2002). "The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain". The Journal of Biological Chemistry. 277 (11): 9212–8. doi:10.1074/jbc.M112414200. PMID 11773082.
  • Hattula K, Furuhjelm J, Arffman A, Peränen J (Sep 2002). "A Rab8-specific GDP/GTP exchange factor is involved in actin remodeling and polarized membrane transport". Molecular Biology of the Cell. 13 (9): 3268–80. doi:10.1091/mbc.E02-03-0143. PMC 124888. PMID 12221131.
  • 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.
  • Lau AS, Mruk DD (Apr 2003). "Rab8B GTPase and junction dynamics in the testis". Endocrinology. 144 (4): 1549–63. doi:10.1210/en.2002-220893. PMID 12639940.
  • Linder MD, Uronen RL, Hölttä-Vuori M, van der Sluijs P, Peränen J, Ikonen E (Jan 2007). "Rab8-dependent recycling promotes endosomal cholesterol removal in normal and sphingolipidosis cells". Molecular Biology of the Cell. 18 (1): 47–56. doi:10.1091/mbc.E06-07-0575. PMC 1751315. PMID 17050734.
  • v
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  • 2fu5: structure of Rab8 in complex with MSS4
    2fu5: structure of Rab8 in complex with MSS4


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