SNAPAP: Difference between revisions

Jump to navigation Jump to search
VisualWikitext
WikiBot (talk | contribs)
Bots, Bureaucrats, bureaucrats, interwiki, nocaptcha, Administrators
57,550 edits
m Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +)
 
 
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''SNARE-associated protein Snapin''' is a [[protein]] that in humans is encoded by the ''SNAPIN'' [[gene]].<ref name="pmid10195194">{{cite journal | vauthors = Ilardi JM, Mochida S, Sheng ZH | title = Snapin: a SNARE-associated protein implicated in synaptic transmission | journal = Nature Neuroscience | volume = 2 | issue = 2 | pages = 119–24 | date = Feb 1999 | pmid = 10195194 | pmc =  | doi = 10.1038/5673 }}</ref><ref name="pmid12659861">{{cite journal | vauthors = Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH | title = Snapin interacts with the N-terminus of regulator of G protein signaling 7 | journal = Biochemical and Biophysical Research Communications | volume = 303 | issue = 2 | pages = 594–9 | date = Apr 2003 | pmid = 12659861 | pmc =  | doi = 10.1016/S0006-291X(03)00400-5 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: SNAPAP SNAP-associated protein| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23557| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = SNAP-associated protein
| HGNCid = 17145
| Symbol = SNAPAP
| AltSymbols =; SNAPIN
| OMIM = 607007
| ECnumber = 
| Homologene = 8251
| MGIid = 1333745
| Function = {{GNF_GO|id=GO:0000149 |text = SNARE binding}}
| Component = {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0008021 |text = synaptic vesicle}} {{GNF_GO|id=GO:0019717 |text = synaptosome}} {{GNF_GO|id=GO:0045202 |text = synapse}}
| Process = {{GNF_GO|id=GO:0006886 |text = intracellular protein transport}} {{GNF_GO|id=GO:0006887 |text = exocytosis}} {{GNF_GO|id=GO:0007269 |text = neurotransmitter secretion}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 23557
    | Hs_Ensembl = ENSG00000143553
    | Hs_RefseqProtein = NP_036569
    | Hs_RefseqmRNA = NM_012437
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 151897754
    | Hs_GenLoc_end = 151900930
    | Hs_Uniprot = O95295
    | Mm_EntrezGene = 20615
    | Mm_Ensembl = ENSMUSG00000001018
    | Mm_RefseqmRNA = NM_133854
    | Mm_RefseqProtein = NP_598615
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 90573961
    | Mm_GenLoc_end = 90576931
    | Mm_Uniprot = Q3UY32
  }}
}}
'''SNAP-associated protein''', also known as '''SNAPAP''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNAPAP SNAP-associated protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23557| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
SNAPAP is a component of the SNARE complex of proteins that is required for synaptic vesicle docking and fusion.<ref name="pmid10195194"/> 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.<ref name="entrez"/><ref name="pmid15102850"/>
{{PBB_Summary
| section_title =
| summary_text = 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]<ref name="entrez">{{cite web | title = Entrez Gene: SNAPAP SNAP-associated protein| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23557| accessdate = }}</ref>
}}


==References==
Snapin has been established to be a promoter of vesicle docking, as it plays a role in binding to [[SNAP-25]], which together stabilize and favor [[SNARE (protein)|SNARE complex]] assembly and vesicle docking.<ref name="pmid23469084">{{cite journal | vauthors = Yu SC, Klosterman SM, Martin AA, Gracheva EO, Richmond JE | title = Differential roles for snapin and synaptotagmin in the synaptic vesicle cycle | journal = PLOS ONE | volume = 8 | issue = 2 | pages = e57842 | year = 2013 | pmid = 23469084 | pmc = 3585204 | doi = 10.1371/journal.pone.0057842 }}</ref> Specifically, the degree to which snapin is necessary for proper synaptic release varies across species. The functions of snapin have been reported to be independent of [[synaptotagmin]], and works through the [[SNAP-25]] pathway to stabilize, prime, and dock vesicles.<ref name="pmid23469084"/>
{{reflist|2}}
 
==Further reading==
== Interactions ==
{{refbegin | 2}}
 
{{PBB_Further_reading
SNAPAP has been shown to [[Protein-protein interaction|interact]] with:
| citations =  
{{div col|colwidth=20em}}
*{{cite journal  | author=Ilardi JM, Mochida S, Sheng ZH |title=Snapin: a SNARE-associated protein implicated in synaptic transmission. |journal=Nat. Neurosci. |volume=2 |issue= 2 |pages= 119-24 |year= 1999 |pmid= 10195194 |doi= 10.1038/5673 }}
* [[BLOC1S1]],<ref name = pmid15102850>{{cite journal | vauthors = Starcevic M, Dell'Angelica EC | title = 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) | journal = The Journal of Biological Chemistry | volume = 279 | issue = 27 | pages = 28393–401 | date = Jul 2004 | pmid = 15102850 | doi = 10.1074/jbc.M402513200 }}</ref>
*{{cite journal | author=Chheda MG, Ashery U, Thakur P, ''et al.'' |title=Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex. |journal=Nat. Cell Biol. |volume=3 |issue= 4 |pages= 331-8 |year= 2001 |pmid= 11283605 |doi= 10.1038/35070000 }}
* [[BLOC1S2]],<ref name = pmid15102850/>
*{{cite journal  | author=Moriyama K, Bonifacino JS |title=Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles. |journal=Traffic |volume=3 |issue= 9 |pages= 666-77 |year= 2003 |pmid= 12191018 |doi= }}
* [[Dysbindin]],<ref name = pmid15102850/>
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
* [[PLDN]],<ref name = pmid15102850/>
*{{cite journal  | author=Ciciotte SL, Gwynn B, Moriyama K, ''et al.'' |title=Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1). |journal=Blood |volume=101 |issue= 11 |pages= 4402-7 |year= 2003 |pmid= 12576321 |doi= 10.1182/blood-2003-01-0020 }}
* [[RGS7]],<ref name = pmid12659861 />
*{{cite journal | author=Hunt RA, Edris W, Chanda PK, ''et al.'' |title=Snapin interacts with the N-terminus of regulator of G protein signaling 7. |journal=Biochem. Biophys. Res. Commun. |volume=303 |issue= 2 |pages= 594-9 |year= 2003 |pmid= 12659861 |doi= }}
* [[SNAP-25]],<ref name = pmid10195194 />
*{{cite journal | author=Battle MA, Maher VM, McCormick JJ |title=ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways. |journal=Biochemistry |volume=42 |issue= 24 |pages= 7270-82 |year= 2003 |pmid= 12809483 |doi= 10.1021/bi034081y }}
* [[SNAP23]],<ref name = pmid12877659>{{cite journal | vauthors = Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T | title = Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells | journal = The Biochemical Journal | volume = 375 | issue = Pt 2 | pages = 433–40 | date = Oct 2003 | pmid = 12877659 | pmc = 1223698 | doi = 10.1042/BJ20030427 }}</ref>  and
*{{cite journal | author=Buxton P, Zhang XM, Walsh B, ''et al.'' |title=Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells. |journal=Biochem. J. |volume=375 |issue= Pt 2 |pages= 433-40 |year= 2004 |pmid= 12877659 |doi= 10.1042/BJ20030427 }}
* [[TRPV1]].<ref name = pmid15066994>{{cite journal | vauthors = Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A | title = Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity | journal = The Journal of Biological Chemistry | volume = 279 | issue = 24 | pages = 25665–72 | date = Jun 2004 | pmid = 15066994 | doi = 10.1074/jbc.M311515200 }}</ref>
*{{cite journal | author=Li W, Zhang Q, Oiso N, ''et al.'' |title=Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1). |journal=Nat. Genet. |volume=35 |issue= 1 |pages= 84-9 |year= 2003 |pmid= 12923531 |doi= 10.1038/ng1229 }}
{{Div col end}}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
 
*{{cite journal | author=Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A |title=Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity. |journal=J. Biol. Chem. |volume=279 |issue= 24 |pages= 25665-72 |year= 2004 |pmid= 15066994 |doi= 10.1074/jbc.M311515200 }}
== References ==
*{{cite journal | author=Starcevic M, Dell'Angelica EC |title=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). |journal=J. Biol. Chem. |volume=279 |issue= 27 |pages= 28393-401 |year= 2004 |pmid= 15102850 |doi= 10.1074/jbc.M402513200 }}
{{reflist|33em}}
*{{cite journal | author=Colland F, Jacq X, Trouplin V, ''et al.'' |title=Functional proteomics mapping of a human signaling pathway. |journal=Genome Res. |volume=14 |issue= 7 |pages= 1324-32 |year= 2004 |pmid= 15231748 |doi= 10.1101/gr.2334104 }}
 
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
== Further reading ==
*{{cite journal | author=Schaaf CP, Benzing J, Schmitt T, ''et al.'' |title=Novel interaction partners of the TPR/MET tyrosine kinase. |journal=FASEB J. |volume=19 |issue= 2 |pages= 267-9 |year= 2005 |pmid= 15546961 |doi= 10.1096/fj.04-1558fje }}
{{refbegin|33em}}
*{{cite journal | author=Rüder C, Reimer T, Delgado-Martinez I, ''et al.'' |title=EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin. |journal=Mol. Biol. Cell |volume=16 |issue= 3 |pages= 1245-57 |year= 2005 |pmid= 15635093 |doi= 10.1091/mbc.E04-09-0817 }}
* {{cite journal | vauthors = Chheda MG, Ashery U, Thakur P, Rettig J, Sheng ZH | title = Phosphorylation of Snapin by PKA modulates its interaction with the SNARE complex | journal = Nature Cell Biology | volume = 3 | issue = 4 | pages = 331–8 | date = Apr 2001 | pmid = 11283605 | doi = 10.1038/35070000 }}
*{{cite journal | author=Pope SN, Lee IR |title=Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin. |journal=J. Steroid Biochem. Mol. Biol. |volume=94 |issue= 1-3 |pages= 203-8 |year= 2005 |pmid= 15862967 |doi= 10.1016/j.jsbmb.2005.01.007 }}
* {{cite journal | vauthors = Moriyama K, Bonifacino JS | title = Pallidin is a component of a multi-protein complex involved in the biogenesis of lysosome-related organelles | journal = Traffic | volume = 3 | issue = 9 | pages = 666–77 | date = Sep 2002 | pmid = 12191018 | doi = 10.1034/j.1600-0854.2002.30908.x }}
*{{cite journal | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
* {{cite journal | vauthors = Ciciotte SL, Gwynn B, Moriyama K, Huizing M, Gahl WA, Bonifacino JS, Peters LL | title = Cappuccino, a mouse model of Hermansky-Pudlak syndrome, encodes a novel protein that is part of the pallidin-muted complex (BLOC-1) | journal = Blood | volume = 101 | issue = 11 | pages = 4402–7 | date = Jun 2003 | pmid = 12576321 | doi = 10.1182/blood-2003-01-0020 }}
*{{cite journal | author=Talbot K, Cho DS, Ong WY, ''et al.'' |title=Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin. |journal=Hum. Mol. Genet. |volume=15 |issue= 20 |pages= 3041-54 |year= 2006 |pmid= 16980328 |doi= 10.1093/hmg/ddl246 }}
* {{cite journal | vauthors = Battle MA, Maher VM, McCormick JJ | title = ST7 is a novel low-density lipoprotein receptor-related protein (LRP) with a cytoplasmic tail that interacts with proteins related to signal transduction pathways | journal = Biochemistry | volume = 42 | issue = 24 | pages = 7270–82 | date = Jun 2003 | pmid = 12809483 | doi = 10.1021/bi034081y }}
*{{cite journal  | author=Suzuki F, Morishima S, Tanaka T, Muramatsu I |title=Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6. |journal=J. Biol. Chem. |volume=282 |issue= 40 |pages= 29563-73 |year= 2007 |pmid= 17684020 |doi= 10.1074/jbc.M702063200 }}
* {{cite journal | vauthors = Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T | title = Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells | journal = The Biochemical Journal | volume = 375 | issue = Pt 2 | pages = 433–40 | date = Oct 2003 | pmid = 12877659 | pmc = 1223698 | doi = 10.1042/BJ20030427 }}
}}
* {{cite journal | vauthors = Li W, Zhang Q, Oiso N, Novak EK, Gautam R, O'Brien EP, Tinsley CL, Blake DJ, Spritz RA, Copeland NG, Jenkins NA, Amato D, Roe BA, Starcevic M, Dell'Angelica EC, Elliott RW, Mishra V, Kingsmore SF, Paylor RE, Swank RT | title = Hermansky-Pudlak syndrome type 7 (HPS-7) results from mutant dysbindin, a member of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) | journal = Nature Genetics | volume = 35 | issue = 1 | pages = 84–9 | date = Sep 2003 | pmid = 12923531 | pmc = 2860733 | doi = 10.1038/ng1229 }}
* {{cite journal | vauthors = Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A | title = Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity | journal = The Journal of Biological Chemistry | volume = 279 | issue = 24 | pages = 25665–72 | date = Jun 2004 | pmid = 15066994 | doi = 10.1074/jbc.M311515200 }}
* {{cite journal | vauthors = Starcevic M, Dell'Angelica EC | title = 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) | journal = The Journal of Biological Chemistry | volume = 279 | issue = 27 | pages = 28393–401 | date = Jul 2004 | pmid = 15102850 | doi = 10.1074/jbc.M402513200 }}
* {{cite journal | vauthors = Colland F, Jacq X, Trouplin V, Mougin C, Groizeleau C, Hamburger A, Meil A, Wojcik J, Legrain P, Gauthier JM | title = Functional proteomics mapping of a human signaling pathway | journal = Genome Research | volume = 14 | issue = 7 | pages = 1324–32 | date = Jul 2004 | pmid = 15231748 | pmc = 442148 | doi = 10.1101/gr.2334104 }}
* {{cite journal | vauthors = Schaaf CP, Benzing J, Schmitt T, Erz DH, Tewes M, Bartram CR, Janssen JW | title = Novel interaction partners of the TPR/MET tyrosine kinase | journal = FASEB Journal | volume = 19 | issue = 2 | pages = 267–9 | date = Feb 2005 | pmid = 15546961 | doi = 10.1096/fj.04-1558fje }}
* {{cite journal | vauthors = Rüder C, Reimer T, Delgado-Martinez I, Hermosilla R, Engelsberg A, Nehring R, Dörken B, Rehm A | title = EBAG9 adds a new layer of control on large dense-core vesicle exocytosis via interaction with Snapin | journal = Molecular Biology of the Cell | volume = 16 | issue = 3 | pages = 1245–57 | date = Mar 2005 | pmid = 15635093 | pmc = 551489 | doi = 10.1091/mbc.E04-09-0817 }}
* {{cite journal | vauthors = Pope SN, Lee IR | title = Yeast two-hybrid identification of prostatic proteins interacting with human sex hormone-binding globulin | journal = The Journal of Steroid Biochemistry and Molecular Biology | volume = 94 | issue = 1-3 | pages = 203–8 | date = Feb 2005 | pmid = 15862967 | doi = 10.1016/j.jsbmb.2005.01.007 }}
* {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | date = Sep 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}
* {{cite journal | vauthors = Talbot K, Cho DS, Ong WY, Benson MA, Han LY, Kazi HA, Kamins J, Hahn CG, Blake DJ, Arnold SE | title = Dysbindin-1 is a synaptic and microtubular protein that binds brain snapin | journal = Human Molecular Genetics | volume = 15 | issue = 20 | pages = 3041–54 | date = Oct 2006 | pmid = 16980328 | doi = 10.1093/hmg/ddl246 }}
* {{cite journal | vauthors = Suzuki F, Morishima S, Tanaka T, Muramatsu I | title = Snapin, a new regulator of receptor signaling, augments alpha1A-adrenoceptor-operated calcium influx through TRPC6 | journal = The Journal of Biological Chemistry | volume = 282 | issue = 40 | pages = 29563–73 | date = Oct 2007 | pmid = 17684020 | doi = 10.1074/jbc.M702063200 }}
{{refend}}
{{refend}}


{{protein-stub}}
 
{{WikiDoc Sources}}
{{gene-1-stub}}

Latest revision as of 06:44, 11 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

Function

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.[3][4]

Snapin has been established to be a promoter of vesicle docking, as it plays a role in binding to SNAP-25, which together stabilize and favor SNARE complex assembly and vesicle docking.[5] Specifically, the degree to which snapin is necessary for proper synaptic release varies across species. The functions of snapin have been reported to be independent of synaptotagmin, and works through the SNAP-25 pathway to stabilize, prime, and dock vesicles.[5]

Interactions

SNAPAP has been shown to interact with:

References

  1. ↑ 1.0 1.1 1.2 Ilardi JM, Mochida S, Sheng ZH (Feb 1999). "Snapin: a SNARE-associated protein implicated in synaptic transmission". Nature Neuroscience. 2 (2): 119–24. doi:10.1038/5673. PMID 10195194.
  2. ↑ 2.0 2.1 Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH (Apr 2003). "Snapin interacts with the N-terminus of regulator of G protein signaling 7". Biochemical and Biophysical Research Communications. 303 (2): 594–9. doi:10.1016/S0006-291X(03)00400-5. PMID 12659861.
  3. ↑ 3.0 3.1 "Entrez Gene: SNAPAP SNAP-associated protein".
  4. ↑ 4.0 4.1 4.2 4.3 4.4 Starcevic M, Dell'Angelica EC (Jul 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)". The Journal of Biological Chemistry. 279 (27): 28393–401. doi:10.1074/jbc.M402513200. PMID 15102850.
  5. ↑ 5.0 5.1 Yu SC, Klosterman SM, Martin AA, Gracheva EO, Richmond JE (2013). "Differential roles for snapin and synaptotagmin in the synaptic vesicle cycle". PLOS ONE. 8 (2): e57842. doi:10.1371/journal.pone.0057842. PMC 3585204. PMID 23469084.
  6. ↑ Buxton P, Zhang XM, Walsh B, Sriratana A, Schenberg I, Manickam E, Rowe T (Oct 2003). "Identification and characterization of Snapin as a ubiquitously expressed SNARE-binding protein that interacts with SNAP23 in non-neuronal cells". The Biochemical Journal. 375 (Pt 2): 433–40. doi:10.1042/BJ20030427. PMC 1223698. PMID 12877659.
  7. ↑ Morenilla-Palao C, Planells-Cases R, García-Sanz N, Ferrer-Montiel A (Jun 2004). "Regulated exocytosis contributes to protein kinase C potentiation of vanilloid receptor activity". The Journal of Biological Chemistry. 279 (24): 25665–72. doi:10.1074/jbc.M311515200. PMID 15066994.

Further reading


Retrieved from "https://www.wikidoc.org/index.php?title=SNAPAP&oldid=1411129"