SNAPAP

From Wikipedia, the free encyclopedia

SNAP-associated protein

Identifiers

External IDs

OMIM: 607007 MGI: 1333745 HomoloGene: 8251

Gene ontology
Molecular Function:	• SNARE binding
Cellular Component:	• cytosol • synaptic vesicle • synaptosome • synapse
Biological Process:	• intracellular protein transport • exocytosis • neurotransmitter secretion

Orthologs

Human

Mouse

Refseq

NM_012437 (mRNA)
NP_036569 (protein)

NM_133854 (mRNA)
NP_598615 (protein)

Location

Chr 1: 151.9 - 151.9 Mb

Chr 3: 90.57 - 90.58 Mb

Pubmed search

[1]

[2]

SNAP-associated protein, also known as SNAPAP, is a human gene.^[1]

SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion (Ilardi et al., 1999). SNAPAP is also a component of the ubiquitously expressed BLOC1 multisubunit protein complex. BLOC1 is required for normal biogenesis of specialized organelles of the endosomal-lysosomal system, such as melanosomes and platelet dense granules (Starcevic and Dell'Angelica, 2004).[supplied by OMIM]^[1]

[edit] References

^ ^a ^b Entrez Gene: SNAPAP SNAP-associated protein.

[edit] Further reading

Ilardi JM, Mochida S, Sheng ZH (1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission.". Nat. Neurosci. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
Chheda MG, Ashery U, Thakur P, et al. (2001). "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex.". Nat. Cell Biol. 3 (4): 331–8. doi:10.1038/35070000. PMID 11283605.
Moriyama K, Bonifacino JS (2003). "Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles.". Traffic 3 (9): 666–77. PMID 12191018.
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. doi:10.1073/pnas.242603899. PMID 12477932.
Ciciotte SL, Gwynn B, Moriyama K, et al. (2003). "Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1).". Blood 101 (11): 4402–7. doi:10.1182/blood-2003-01-0020. PMID 12576321.
Hunt RA, Edris W, Chanda PK, et al. (2003). "Snapin interacts with the N-terminus of regulator of G protein signaling 7.". Biochem. Biophys. Res. Commun. 303 (2): 594–9. PMID 12659861.
Battle MA, Maher VM, McCormick JJ (2003). "ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways.". Biochemistry 42 (24): 7270–82. doi:10.1021/bi034081y. PMID 12809483.
Buxton P, Zhang XM, Walsh B, et al. (2004). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells.". Biochem. J. 375 (Pt 2): 433–40. doi:10.1042/BJ20030427. PMID 12877659.
Li W, Zhang Q, Oiso N, et al. (2003). "Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1).". Nat. Genet. 35 (1): 84–9. doi:10.1038/ng1229. PMID 12923531.
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.
Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A (2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity.". J. Biol. Chem. 279 (24): 25665–72. doi:10.1074/jbc.M311515200. PMID 15066994.
Starcevic M, Dell'Angelica EC (2004). "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1).". J. Biol. Chem. 279 (27): 28393–401. doi:10.1074/jbc.M402513200. PMID 15102850.
Colland F, Jacq X, Trouplin V, et al. (2004). "Functional proteomics mapping of a human signaling pathway.". Genome Res. 14 (7): 1324–32. doi:10.1101/gr.2334104. PMID 15231748.
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. PMID 15489334.
Schaaf CP, Benzing J, Schmitt T, et al. (2005). "Novel interaction partners of the TPR/MET tyrosine kinase.". FASEB J. 19 (2): 267–9. doi:10.1096/fj.04-1558fje. PMID 15546961.
Rüder C, Reimer T, Delgado-Martinez I, et al. (2005). "EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin.". Mol. Biol. Cell 16 (3): 1245–57. doi:10.1091/mbc.E04-09-0817. PMID 15635093.
Pope SN, Lee IR (2005). "Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin.". J. Steroid Biochem. Mol. Biol. 94 (1-3): 203–8. doi:10.1016/j.jsbmb.2005.01.007. PMID 15862967.
Stelzl U, Worm U, Lalowski M, et al. (2005). "A human protein-protein interaction network: a resource for annotating the proteome.". Cell 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID 16169070.
Talbot K, Cho DS, Ong WY, et al. (2006). "Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin.". Hum. Mol. Genet. 15 (20): 3041–54. doi:10.1093/hmg/ddl246. PMID 16980328.
Suzuki F, Morishima S, Tanaka T, Muramatsu I (2007). "Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6.". J. Biol. Chem. 282 (40): 29563–73. doi:10.1074/jbc.M702063200. PMID 17684020.