SNAPAP

SNAP-associated protein

Identifiers

External IDs

OMIM: 607007 MGI: 1333745 HomoloGene: 8251 GeneCards: SNAPIN Gene

Gene Ontology
Molecular function	• SNARE binding • protein binding
Cellular component	• cytoplasm • cytosol • synaptic vesicle • membrane • synaptosome • cell junction • cytoplasmic vesicle membrane • synaptic vesicle membrane • BLOC-1 complex • cytoplasmic vesicle • synapse • perinuclear region of cytoplasm
Biological process	• intracellular protein transport • neurotransmitter secretion • synaptic vesicle exocytosis
Sources: Amigo / QuickGO

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
153.63 – 153.63 Mb

Chr 3:
90.29 – 90.29 Mb

PubMed search

[1]

[2]

SNARE-associated protein Snapin is a protein that in humans is encoded by the SNAPIN gene.^[1]^[2]^[3]

SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion.^[1] 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.^[4][supplied by OMIM]^[3]

Interactions

SNAPAP has been shown to interact with SNAP-25,^[1] BLOC1S1,^[4] SNAP23,^[5] Dysbindin,^[4] TRPV1,^[6] PLDN,^[4] BLOC1S2^[4] and RGS7.^[2]

References

^ ^a ^b ^c Ilardi JM, Mochida S, Sheng ZH (April 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nat Neurosci 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
^ ^a ^b Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH (March 2003). "Snapin interacts with the N-terminus of regulator of G protein signaling 7". Biochem Biophys Res Commun 303 (2): 594–9. doi:10.1016/S0006-291X(03)00400-5. PMID 12659861.
^ ^a ^b "Entrez Gene: SNAPAP SNAP-associated protein". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23557.
^ ^a ^b ^c ^d ^e Starcevic, Marta; Dell'Angelica Esteban C (July 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. (United States) 279 (27): 28393–401. doi:10.1074/jbc.M402513200. ISSN 0021-9258. PMID 15102850.
^ Buxton, Penelope; Zhang Xiang-Ming, Walsh Bong, Sriratana Absorn, Schenberg Irina, Manickam Elizabeth, Rowe Tony (October 2003). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". Biochem. J. (England) 375 (Pt 2): 433–40. doi:10.1042/BJ20030427. PMC 1223698. PMID 12877659. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223698.
^ Morenilla-Palao, Cruz; Planells-Cases Rosa, García-Sanz Nuria, Ferrer-Montiel Antonio (June 2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". J. Biol. Chem. (United States) 279 (24): 25665–72. doi:10.1074/jbc.M311515200. ISSN 0021-9258. PMID 15066994.

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. doi:10.1034/j.1600-0854.2002.30908.x. 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. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
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.
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. PMC 1223698. PMID 12877659. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1223698.
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. PMC 2860733. PMID 12923531. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2860733.
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. PMC 442148. PMID 15231748. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=442148.
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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
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. PMC 551489. PMID 15635093. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=551489.
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.

SNAPAP

Interactions

References

Further reading