RAB9A

Protein-coding gene in the species Homo sapiens
RAB9A
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1WMS

Identifiers
AliasesRAB9A, RAB9, member RAS oncogene family
External IDsOMIM: 300284; MGI: 1890695; HomoloGene: 20900; GeneCards: RAB9A; OMA:RAB9A - orthologs
Gene location (Human)
X chromosome (human)
Chr.X chromosome (human)[1]
X chromosome (human)
Genomic location for RAB9A
Genomic location for RAB9A
BandXp22.2Start13,689,128 bp[1]
End13,710,504 bp[1]
Gene location (Mouse)
X chromosome (mouse)
Chr.X chromosome (mouse)[2]
X chromosome (mouse)
Genomic location for RAB9A
Genomic location for RAB9A
BandX|X F5Start165,240,249 bp[2]
End165,262,863 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • amniotic fluid

  • parotid gland

  • palpebral conjunctiva

  • corpus callosum

  • right adrenal cortex

  • skin of hip

  • epithelium of nasopharynx

  • left adrenal gland

  • skin of thigh

  • left adrenal cortex
Top expressed in
  • trigeminal ganglion

  • mucous cell of stomach

  • epithelium of small intestine

  • medial ganglionic eminence

  • left lobe of liver

  • epithelium of stomach

  • brown adipose tissue

  • calvaria

  • genital tubercle

  • left lung lobe
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • nucleotide binding
  • GDP binding
  • GTP binding
  • protein binding
  • GTPase activity
  • identical protein binding
Cellular component
  • endosome
  • late endosome
  • phagocytic vesicle membrane
  • Golgi apparatus
  • endoplasmic reticulum membrane
  • membrane
  • Golgi membrane
  • plasma membrane
  • phagocytic vesicle
  • endoplasmic reticulum
  • lysosome
  • extracellular exosome
  • cytoplasmic vesicle
  • cytoplasmic vesicle membrane
  • trans-Golgi network membrane
  • cytosol
  • transport vesicle
  • melanosome
Biological process
  • regulation of protein localization
  • retrograde transport, endosome to Golgi
  • protein transport
  • positive regulation of exocytosis
  • transport
  • intracellular protein transport
  • Rab protein signal transduction
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9367

56382

Ensembl

ENSG00000123595

ENSMUSG00000079316

UniProt

P51151

Q9R0M6

RefSeq (mRNA)

NM_004251
NM_001195328

NM_019773

RefSeq (protein)

NP_001182257
NP_004242

NP_062747

Location (UCSC)Chr X: 13.69 – 13.71 MbChr X: 165.24 – 165.26 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Ras-related protein Rab-9A is a protein that in humans is encoded by the RAB9A gene.[5][6]

Interactions

RAB9A has been shown to interact with RABEPK,[7] TIP47[8] and the Biogenesis of lysosome-related organelles complex 3.[9]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000123595 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079316 – 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. ^ Davies JP, Cotter PD, Ioannou YA (May 1997). "Cloning and mapping of human Rab7 and Rab9 cDNA sequences and identification of a Rab9 pseudogene". Genomics. 41 (1): 131–4. doi:10.1006/geno.1997.4644. PMID 9126495.
  6. ^ "Entrez Gene: RAB9A RAB9A, member RAS oncogene family".
  7. ^ Díaz E, Schimmöller F, Pfeffer SR (July 1997). "A novel Rab9 effector required for endosome-to-TGN transport". J. Cell Biol. 138 (2): 283–90. doi:10.1083/jcb.138.2.283. PMC 2138197. PMID 9230071.
  8. ^ Carroll KS, Hanna J, Simon I, Krise J, Barbero P, Pfeffer SR (May 2001). "Role of Rab9 GTPase in facilitating receptor recruitment by TIP47". Science. 292 (5520): 1373–6. Bibcode:2001Sci...292.1373C. doi:10.1126/science.1056791. PMID 11359012. S2CID 31343936.
  9. ^ Kloer DP, Rojas R, Ivan V, Moriyama K, van Vlijmen T, Murthy N, Ghirlando R, van der Sluijs P, Hurley JH, Bonifacino JS (March 2010). "Assembly of the biogenesis of lysosome-related organelles complex-3 (BLOC-3) and its interaction with Rab9". J. Biol. Chem. 285 (10): 7794–7804. doi:10.1074/jbc.M109.069088. PMC 2844223. PMID 20048159.

Further reading

  • Shapiro AD, Pfeffer SR (1995). "Quantitative analysis of the interactions between prenyl Rab9, GDP dissociation inhibitor-alpha, and guanine nucleotides". J. Biol. Chem. 270 (19): 11085–90. doi:10.1074/jbc.270.19.11085. PMID 7744738.
  • Soldati T, Riederer MA, Pfeffer SR (1993). "Rab GDI: a solubilizing and recycling factor for rab9 protein". Mol. Biol. Cell. 4 (4): 425–34. doi:10.1091/mbc.4.4.425. PMC 300943. PMID 8389620.
  • Díaz E, Schimmöller F, Pfeffer SR (1997). "A novel Rab9 effector required for endosome-to-TGN transport". J. Cell Biol. 138 (2): 283–90. doi:10.1083/jcb.138.2.283. PMC 2138197. PMID 9230071.
  • de Leeuw HP, Koster PM, Calafat J, Janssen H, van Zonneveld AJ, van Mourik JA, Voorberg J (1998). "Small GTP-binding proteins in human endothelial cells". Br. J. Haematol. 103 (1): 15–9. doi:10.1046/j.1365-2141.1998.00965.x. PMID 9792283. S2CID 24857520.
  • Shisheva A, Chinni SR, DeMarco C (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.
  • Carroll KS, Hanna J, Simon I, Krise J, Barbero P, Pfeffer SR (2001). "Role of Rab9 GTPase in facilitating receptor recruitment by TIP47". Science. 292 (5520): 1373–6. Bibcode:2001Sci...292.1373C. doi:10.1126/science.1056791. PMID 11359012. S2CID 31343936.
  • Orzaez D, de Jong AJ, Woltering EJ (2001). "A tomato homologue of the human protein PIRIN is induced during programmed cell death". Plant Mol. Biol. 46 (4): 459–68. doi:10.1023/A:1010618515051. PMID 11485202. S2CID 8587440.
  • Michel F, Soler-Lopez M, Petosa C, Cramer P, Siebenlist U, Müller CW (2002). "Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family". EMBO J. 20 (22): 6180–90. doi:10.1093/emboj/20.22.6180. PMC 125740. PMID 11707390.
  • Barbero P, Bittova L, Pfeffer SR (2002). "Visualization of Rab9-mediated vesicle transport from endosomes to the trans-Golgi in living cells". J. Cell Biol. 156 (3): 511–8. doi:10.1083/jcb.200109030. PMC 2173336. PMID 11827983.
  • Hanna J, Carroll K, Pfeffer SR (2002). "Identification of residues in TIP47 essential for Rab9 binding". Proc. Natl. Acad. Sci. U.S.A. 99 (11): 7450–4. Bibcode:2002PNAS...99.7450H. doi:10.1073/pnas.112198799. PMC 124251. PMID 12032303.
  • Walter M, Davies JP, Ioannou YA (2004). "Telomerase immortalization upregulates Rab9 expression and restores LDL cholesterol egress from Niemann-Pick C1 late endosomes". J. Lipid Res. 44 (2): 243–53. doi:10.1194/jlr.M200230-JLR200. PMID 12576506.
  • Seaman MN (2004). "Cargo-selective endosomal sorting for retrieval to the Golgi requires retromer". J. Cell Biol. 165 (1): 111–22. doi:10.1083/jcb.200312034. PMC 2172078. PMID 15078902.
  • Chen L, DiGiammarino E, Zhou XE, Wang Y, Toh D, Hodge TW, Meehan EJ (2004). "High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target". J. Biol. Chem. 279 (38): 40204–8. doi:10.1074/jbc.M407114200. PMID 15263003.
  • Ganley IG, Carroll K, Bittova L, Pfeffer S (2005). "Rab9 GTPase regulates late endosome size and requires effector interaction for its stability". Mol. Biol. Cell. 15 (12): 5420–30. doi:10.1091/mbc.E04-08-0747. PMC 532021. PMID 15456905.
  • Ganley IG, Pfeffer SR (2006). "Cholesterol accumulation sequesters Rab9 and disrupts late endosome function in NPC1-deficient cells". J. Biol. Chem. 281 (26): 17890–9. doi:10.1074/jbc.M601679200. PMC 3650718. PMID 16644737.
  • Aivazian D, Serrano RL, Pfeffer S (2006). "TIP47 is a key effector for Rab9 localization". J. Cell Biol. 173 (6): 917–26. doi:10.1083/jcb.200510010. PMC 2063917. PMID 16769818.
  • v
  • t
  • e
  • 1s8f: Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
    1s8f: Crystal structure of Rab9 complexed to GDP reveals a dimer with an active conformation of switch II
  • 1wms: High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target
    1wms: High resolution crystal structure of human Rab9 GTPase: a novel antiviral drug target
  • 1yzl: GppNHp-Bound Rab9 GTPase
    1yzl: GppNHp-Bound Rab9 GTPase


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