GTPBP4

GTPBP4
Identifiers
Aliases	GTPBP4 , CRFG, NGB, NOG1, GTP binding protein 4
External IDs	MGI: 1916487 HomoloGene: 7100 GeneCards: GTPBP4
Gene location (Human) Chr. Chromosome 10 (human) [1] Band 10p15.3 Start 988,434 bp [1] End 1,019,932 bp [1]
Gene location (Mouse) Chr. Chromosome 13 (mouse) [2] Band 13|13 A1 Start 9,016,367 bp [2] End 9,046,119 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in sperm Achilles tendon mucosa of urinary bladder amniotic fluid stromal cell of endometrium gastrocnemius muscle palpebral conjunctiva Left adrenal gland pericardium hair follicle Top expressed in otic placode saccule morula primitive streak blastocyst somite plantaris muscle spermatocyte extensor digitorum longus muscle hair follicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding GTP binding protein binding GTPase activity RNA binding Cellular component cytoplasm Golgi apparatus nuclear membrane membrane nucleolus perinuclear region of cytoplasm nucleus cytosol Biological process regulation of cyclin-dependent protein serine/threonine kinase activity ribosome biogenesis negative regulation of cell-cell adhesion protein stabilization negative regulation of DNA replication negative regulation of protein ubiquitination negative regulation of cell migration osteoblast differentiation negative regulation of collagen binding negative regulation of cell population proliferation maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 23560 69237 Ensembl ENSG00000107937 ENSMUSG00000021149 UniProt Q9BZE4 Q99ME9 RefSeq (mRNA) NM_012341 NM_027000 RefSeq (protein) NP_036473 NP_081276 Location (UCSC) Chr 10: 0.99 – 1.02 Mb Chr 13: 9.02 – 9.05 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Nucleolar GTP-binding protein 1 is a protein that in humans is encoded by the GTPBP4 gene. ^{[5] [6]}

GTPases function as molecular switches that can flip between two states: active, when GTP is bound, and inactive, when GDP is bound. 'Active' usually means that the molecule acts as a signal to trigger other events in the cell. When an extracellular ligand binds to a G protein-coupled receptor, the receptor changes its conformation and switches on the trimeric G proteins that associate with it by causing them to eject their GDP and replace it with GTP. The switch is turned off when the G protein hydrolyzes its own bound GTP, converting it back to GDP. But before that occurs, the active protein has an opportunity to diffuse away from the receptor and deliver its message for a prolonged period to its downstream target. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000107937 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000021149 - 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. Laping NJ, Olson BA, Zhu Y (Apr 2001). "Identification of a novel nuclear guanosine triphosphate-binding protein differentially expressed in renal disease". J Am Soc Nephrol. 12 (5): 883–90. doi: 10.1681/ASN.V125883 . PMID   11316846.
6. "Entrez Gene: GTPBP4 GTP binding protein 4".

Further reading

• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID   8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID   9373149.
• Scherl A, Couté Y, Déon C, et al. (2003). "Functional proteomic analysis of human nucleolus". Mol. Biol. Cell. 13 (11): 4100–9. doi:10.1091/mbc.E02-05-0271. PMC   133617 . PMID   12429849.
• 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.
• 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.
• 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.
• Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–48. doi: 10.1016/j.cell.2006.09.026 . PMID   17081983. S2CID   7827573.
• Lee H, Kim D, Dan HC, et al. (2007). "Identification and characterization of putative tumor suppressor NGB, a GTP-binding protein that interacts with the neurofibromatosis 2 protein". Mol. Cell. Biol. 27 (6): 2103–19. doi:10.1128/MCB.00572-06. PMC   1820506 . PMID   17210637.
• Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.