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GDI2
Identifiers
Aliases	GDI2, HEL-S-46e, RABGDIB, GDP dissociation inhibitor 2
External IDs	OMIM: 600767; MGI: 99845; HomoloGene: 37488; GeneCards: GDI2; OMA:GDI2 - orthologs
Gene location (Human) Chr. Chromosome 10 (human) Band 10p15.1 Start 5,765,223 bp End 5,842,132 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A1 Start 3,588,063 bp End 3,617,871 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa mucosa of ileum mucosa of sigmoid colon corpus epididymis trabecular bone visceral pleura parietal pleura secondary oocyte epithelium of nasopharynx oral cavity Top expressed in saccule otic placode renal corpuscle mandibular prominence maxillary prominence otic vesicle condyle fossa medullary collecting duct internal carotid artery More reference expression data BioGPS n/a
Gene ontology Molecular function Rab GDP-dissociation inhibitor activity GTPase activator activity small GTPase binding protein binding GDP-dissociation inhibitor activity RNA binding Cellular component cytoplasm vesicle cytosol membrane focal adhesion extracellular exosome extracellular region secretory granule lumen azurophil granule lumen Golgi apparatus synapse Biological process positive regulation of GTPase activity protein transport regulation of catalytic activity regulation of small GTPase mediated signal transduction vesicle-mediated transport signal transduction small GTPase mediated signal transduction neutrophil degranulation Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 2665 14569 Ensembl ENSG00000057608 ENSMUSG00000021218 UniProt P50395 Q5SX91 Q61598 RefSeq (mRNA) NM_001494 NM_001115156 NM_008112 RefSeq (protein) NP_001108628 NP_001485 NP_032138 Location (UCSC) Chr 10: 5.77 – 5.84 Mb Chr 13: 3.59 – 3.62 Mb PubMed search
Wikidata
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Rab GDP dissociation inhibitor beta is a protein that in humans is encoded by the GDI2 gene.

GDP dissociation inhibitors are proteins that regulate the GDP-GTP exchange reaction of members of the rab family, small GTP-binding proteins of the ras superfamily, that are involved in vesicular trafficking of molecules between cellular organelles. GDIs slow the rate of dissociation of GDP from rab proteins and release GDP from membrane-bound rabs. GDI2 is ubiquitously expressed. The GDI2 gene contains many repetitive elements indicating that it may be prone to inversion/deletion rearrangements.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000057608 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000021218 – 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. Sedlacek Z, Munstermann E, Mincheva A, Lichter P, Poustka A (Feb 1998). "The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13". Mamm Genome. 9 (1): 78–80. doi:10.1007/s003359900685. PMID 9434952. S2CID 36441100.
6. ^ "Entrez Gene: GDI2 GDP dissociation inhibitor 2".

Further reading

• Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID 1602151.
• Shisheva A, Südhof TC, Czech MP (1994). "Cloning, characterization, and expression of a novel GDP dissociation inhibitor isoform from skeletal muscle". Mol. Cell. Biol. 14 (5): 3459–68. doi:10.1128/mcb.14.5.3459. PMC 358710. PMID 7513052.
• Bächner D, Sedlacek Z, Korn B, et al. (1995). "Expression patterns of two human genes coding for different rab GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved in cellular transport". Hum. Mol. Genet. 4 (4): 701–8. doi:10.1093/hmg/4.4.701. PMID 7543319.
• Nishimura N, Goji J, Nakamura H, et al. (1995). "Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens". Cancer Res. 55 (22): 5445–50. PMID 7585614.
• Shisheva A, Buxton J, Czech MP (1994). "Differential intracellular localizations of GDP dissociation inhibitor isoforms. Insulin-dependent redistribution of GDP dissociation inhibitor-2 in 3T3-L1 adipocytes". J. Biol. Chem. 269 (39): 23865–8. doi:10.1016/S0021-9258(19)51016-X. PMID 7929030.
• Shisheva A, Doxsey SJ, Buxton JM, Czech MP (1996). "Pericentriolar targeting of GDP-dissociation inhibitor isoform 2". Eur. J. Cell Biol. 68 (2): 143–58. PMID 8575461.
• 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.
• Caillol N, Pasqualini E, Lloubes R, Lombardo D (2000). "Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells". J. Cell. Biochem. 79 (4): 628–47. doi:10.1002/1097-4644(20001215)79:4<628::AID-JCB120>3.0.CO;2-T. PMID 10996854. S2CID 11614620.
• Weitzdoerfer R, Stolzlechner D, Dierssen M, et al. (2002). "Reduction of nucleoside diphosphate kinase B, Rab GDP- dissociation inhibitor beta and histidine triad nucleotide-binding protein in fetal Down Syndrome brain". Protein Expression in Down Syndrome Brain. pp. 347–59. doi:10.1007/978-3-7091-6262-0_29. ISBN 978-3-211-83704-7. PMID 11771757. {{cite book}}: |journal= ignored (help)
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Shin BK, Wang H, Yim AM, et al. (2003). "Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function". J. Biol. Chem. 278 (9): 7607–16. doi:10.1074/jbc.M210455200. PMID 12493773.
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
• Theodorescu D, Sapinoso LM, Conaway MR, et al. (2004). "Reduced expression of metastasis suppressor RhoGDI2 is associated with decreased survival for patients with bladder cancer". Clin. Cancer Res. 10 (11): 3800–6. doi:10.1158/1078-0432.CCR-03-0653. PMID 15173088.
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
• Bruneel A, Labas V, Mailloux A, et al. (2006). "Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis". Proteomics. 5 (15): 3876–84. doi:10.1002/pmic.200401239. PMID 16130169. S2CID 26007149.
• Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
• Hu LD, Zou HF, Zhan SX, Cao KM (2007). "Biphasic expression of RhoGDI2 in the progression of breast cancer and its negative relation with lymph node metastasis". Oncol. Rep. 17 (6): 1383–9. doi:10.3892/or.17.6.1383. PMID 17487395.
• Sun ZL, Zhu Y, Wang FQ, et al. (2007). "Serum proteomic-based analysis of pancreatic carcinoma for the identification of potential cancer biomarkers". Biochim. Biophys. Acta. 1774 (6): 764–71. doi:10.1016/j.bbapap.2007.04.001. PMID 17507299.

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