NAPG

NAPG
Identifiers
Aliases	NAPG , GAMMASNAP, NSF attachment protein gamma
External IDs	OMIM: 603216; MGI: 104561; HomoloGene: 2838; GeneCards: NAPG; OMA:NAPG - orthologs
Gene location (Human) Chr. Chromosome 18 (human) [1] Band 18p11.22 Start 10,525,905 bp [1] End 10,552,764 bp [1]
Gene location (Mouse) Chr. Chromosome 18 (mouse) [2] Band 18|18 E1 Start 63,110,902 bp [2] End 63,132,521 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in endothelial cell pons pars compacta Brodmann area 23 islet of Langerhans C1 segment lateral nuclear group of thalamus middle temporal gyrus dorsolateral prefrontal cortex Brodmann area 9 Top expressed in subiculum pontine nuclei piriform cortex central gray substance of midbrain medial dorsal nucleus primary motor cortex inferior colliculi subdivision of hippocampus Region I of hippocampus proper habenula More reference expression data BioGPS More reference expression data
Gene ontology Molecular function syntaxin binding protein binding soluble NSF attachment protein activity Cellular component myelin sheath lysosomal membrane SNARE complex extracellular exosome membrane mitochondrion vacuolar membrane synapse Biological process protein transport protein stabilization membrane fusion intracellular protein transport intra-Golgi vesicle-mediated transport vesicle-mediated transport transport protein-containing complex assembly Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 8774 108123 Ensembl ENSG00000134265 ENSMUSG00000024581 UniProt Q99747 Q9CWZ7 RefSeq (mRNA) NM_003826 NM_028017 RefSeq (protein) NP_003817 NP_082293 Location (UCSC) Chr 18: 10.53 – 10.55 Mb Chr 18: 63.11 – 63.13 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Gamma-soluble NSF attachment protein is a SNAP protein that in humans is encoded by the NAPG gene. ^{[5] [6]}

Function

NSF and SNAPs (NSF attachment proteins) are general elements of the cellular membrane transport apparatus. The sequence of the predicted 312-amino acid human protein encoded by NAPG is 95% identical to that of bovine gamma-SNAP. NAPG mediates platelet exocytosis and controls the membrane fusion events of this process. ^[6]

References

1. GRCh38: Ensembl release 89: ENSG00000134265 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000024581 – 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. Lemons PP, Chen D, Bernstein AM, Bennett MK, Whiteheart SW (Sep 1997). "Regulated secretion in platelets: identification of elements of the platelet exocytosis machinery". Blood. 90 (4): 1490–500. doi: 10.1182/blood.V90.4.1490 . PMID   9269766.
6. "Entrez Gene: NAPG N-ethylmaleimide-sensitive factor attachment protein, gamma".

Further reading

• Wilson DW, Whiteheart SW, Wiedmann M, et al. (1992). "A multisubunit particle implicated in membrane fusion". J. Cell Biol. 117 (3): 531–8. doi:10.1083/jcb.117.3.531. PMC   2289450 . PMID   1315316.
• Whiteheart SW, Brunner M, Wilson DW, et al. (1992). "Soluble N-ethylmaleimide-sensitive fusion attachment proteins (SNAPs) bind to a multi-SNAP receptor complex in Golgi membranes". J. Biol. Chem. 267 (17): 12239–43. doi: 10.1016/S0021-9258(19)49830-X . PMID   1601890.
• Whiteheart SW, Griff IC, Brunner M, et al. (1993). "SNAP family of NSF attachment proteins includes a brain-specific isoform". Nature. 362 (6418): 353–5. Bibcode:1993Natur.362..353W. doi:10.1038/362353a0. PMID   8455721. S2CID   4341471.
• Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID   8619474.
• Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing". Genome Res. 7 (4): 353–8. doi:10.1101/gr.7.4.353. PMC   139146 . PMID   9110174.
• Mastick CC, Falick AL (1997). "Association of N-ethylmaleimide sensitive fusion (NSF) protein and soluble NSF attachment proteins-alpha and -gamma with glucose transporter-4-containing vesicles in primary rat adipocytes". Endocrinology. 138 (6): 2391–7. doi: 10.1210/endo.138.6.5166 . PMID   9165027.
• Subramaniam VN, Loh E, Horstmann H, et al. (2000). "Preferential association of syntaxin 8 with the early endosome" (PDF). J. Cell Sci. 113 (6): 997–1008. doi:10.1242/jcs.113.6.997. PMID   10683148.
• Chen D, Xu W, He P, et al. (2001). "Gaf-1, a gamma -SNAP-binding protein associated with the mitochondria". J. Biol. Chem. 276 (16): 13127–35. doi: 10.1074/jbc.M009424200 . PMID   11278501.
• 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.
• Tani K, Shibata M, Kawase K, et al. (2003). "Mapping of functional domains of gamma-SNAP". J. Biol. Chem. 278 (15): 13531–8. doi: 10.1074/jbc.M213205200 . PMID   12554740.
• 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.
• Rush J, Moritz A, Lee KA, et al. (2005). "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells". Nat. Biotechnol. 23 (1): 94–101. doi:10.1038/nbt1046. PMID   15592455. S2CID   7200157.
• 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.