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SNARE-associated protein Snapin (Biogenesis of lysosome-related organelles complex 1 subunit 7) (BLOC-1 subunit 7) (Synaptosomal-associated protein 25-binding protein) (SNAP-associated protein)

 SNAPN_HUMAN             Reviewed;         136 AA.
O95295; D3DV56; Q5SXU8;
16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
27-SEP-2017, entry version 146.
RecName: Full=SNARE-associated protein Snapin;
AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 7;
Short=BLOC-1 subunit 7;
AltName: Full=Synaptosomal-associated protein 25-binding protein;
Short=SNAP-associated protein;
Name=SNAPIN; Synonyms=BLOC1S7, SNAP25BP, SNAPAP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=10195194; DOI=10.1038/5673;
Ilardi J.M., Mochida S., Sheng Z.-H.;
"Snapin: a SNARE-associated protein implicated in synaptic
transmission.";
Nat. Neurosci. 2:119-124(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung carcinoma, and Melanoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
INTERACTION WITH RGS7.
PubMed=12659861; DOI=10.1016/S0006-291X(03)00400-5;
Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.;
"Snapin interacts with the N-terminus of regulator of G protein
signaling 7.";
Biochem. Biophys. Res. Commun. 303:594-599(2003).
[8]
IDENTIFICATION IN THE BLOC-1 COMPLEX.
PubMed=15102850; DOI=10.1074/jbc.M402513200;
Starcevic M., Dell'Angelica E.C.;
"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. 279:28393-28401(2004).
[9]
INTERACTION WITH CNTRL.
PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
Guha M., Sillibourne J., Doxsey S.J.;
"Centriolin anchoring of exocyst and SNARE complexes at the midbody is
required for secretory-vesicle-mediated abscission.";
Cell 123:75-87(2005).
[10]
FUNCTION.
PubMed=17182842; DOI=10.1091/mbc.E06-12-1066;
Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V.,
Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
Dell'Angelica E.C., Raposo G., Marks M.S.;
"BLOC-1 is required for cargo-specific sorting from vacuolar early
endosomes toward lysosome-related organelles.";
Mol. Biol. Cell 18:768-780(2007).
[11]
FUNCTION IN VESICLE RECYCLING, INTERACTION WITH TOR1A, SUBCELLULAR
LOCATION, AND PHOSPHORYLATION.
PubMed=18167355; DOI=10.1074/jbc.M704097200;
Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.;
"The dystonia-associated protein torsinA modulates synaptic vesicle
recycling.";
J. Biol. Chem. 283:7568-7579(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[14]
SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE
SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=19168546; DOI=10.1093/molehr/gap004;
Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C.,
Kupryjanczyk J., Jaruzelska J.;
"The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1
proteins in human male germ cells.";
Mol. Hum. Reprod. 15:173-179(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-10; THR-14 AND SER-133, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=21102408; DOI=10.1038/emboj.2010.285;
Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
"CSN complex controls the stability of selected synaptic proteins via
a torsinA-dependent process.";
EMBO J. 30:181-193(2011).
[19]
INTERACTION WITH HHV-5 PROTEIN UL70 (MICROBIAL INFECTION).
PubMed=21917956; DOI=10.1128/JVI.05357-11;
Shen A., Lei J., Yang E., Pei Y., Chen Y.C., Gong H., Xiao G., Liu F.;
"Human cytomegalovirus primase UL70 specifically interacts with
cellular factor Snapin.";
J. Virol. 85:11732-11741(2011).
[20]
IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
COMPLEX.
PubMed=22203680; DOI=10.1074/jbc.M111.325746;
Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R.,
Steven A.C., Bonifacino J.S., Hurley J.H.;
"Assembly and architecture of biogenesis of lysosome-related
organelles complex-1 (BLOC-1).";
J. Biol. Chem. 287:5882-5890(2012).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-126 AND SER-133,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
FUNCTION, IDENTIFICATION OF THE BORC COMPLEX, AND SUBCELLULAR
LOCATION.
PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
"BORC, a multisubunit complex that regulates lysosome positioning.";
Dev. Cell 33:176-188(2015).
-!- FUNCTION: Component of the BLOC-1 complex, a complex that is
required for normal biogenesis of lysosome-related organelles
(LRO), such as platelet dense granules and melanosomes. In concert
with the AP-3 complex, the BLOC-1 complex is required to target
membrane protein cargos into vesicles assembled at cell bodies for
delivery into neurites and nerve terminals. The BLOC-1 complex, in
association with SNARE proteins, is also proposed to be involved
in neurite extension. Plays a role in intracellular vesicle
trafficking and synaptic vesicle recycling. May modulate a step
between vesicle priming, fusion and calcium-dependent
neurotransmitter release through its ability to potentiate the
interaction of synaptotagmin with the SNAREs and the plasma-
membrane-associated protein SNAP25. Its phosphorylation state
influences exocytotic protein interactions and may regulate
synaptic vesicle exocytosis. May also have a role in the
mechanisms of SNARE-mediated membrane fusion in non-neuronal cells
(PubMed:17182842, PubMed:18167355). As part of the BORC complex
may play a role in lysosomes movement and localization at the cell
periphery. Associated with the cytosolic face of lysosomes, the
BORC complex may recruit ARL8B and couple lysosomes to microtubule
plus-end-directed kinesin motor (PubMed:25898167).
{ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355,
ECO:0000269|PubMed:25898167}.
-!- SUBUNIT: Component of the biogenesis of lysosome-related
organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2,
BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1,
BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and
SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3
protein complex and membrane protein cargos (PubMed:15102850,
PubMed:22203680). Component of the BLOC-one-related complex (BORC)
which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7,
BORCS8, KXD1 and SNAPIN (PubMed:25898167). Associates with the
SNARE complex. Interacts with CSNK1D, SNAP23 and STX4A but not
with STX1A, VAMP2 and SYT1. Interacts with SNAP25; the interaction
with SNAP25 is increased by its phosphorylation. Interacts with
CNTRL, NANOS1, PUM2 and RGS7 (PubMed:12659861, PubMed:16213214,
PubMed:19168546). Interacts with TOR1A; the interaction is direct
and associates SNAPIN with the CSN complex (PubMed:18167355,
PubMed:21102408). {ECO:0000269|PubMed:12659861,
ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:16213214,
ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546,
ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:22203680,
ECO:0000269|PubMed:25898167}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus/HHV-5 protein UL70. {ECO:0000269|PubMed:21917956}.
-!- INTERACTION:
Q6QNY1:BLOC1S2; NbExp=7; IntAct=EBI-296723, EBI-465872;
Q9UL45:BLOC1S6; NbExp=2; IntAct=EBI-296723, EBI-465781;
Q96L14:CEP170P1; NbExp=4; IntAct=EBI-296723, EBI-743488;
Q96EV8:DTNBP1; NbExp=4; IntAct=EBI-296723, EBI-465804;
O75923:DYSF; NbExp=3; IntAct=EBI-296723, EBI-2799016;
Q5S007:LRRK2; NbExp=5; IntAct=EBI-296723, EBI-5323863;
Q15849-1:SLC14A2; NbExp=5; IntAct=EBI-296723, EBI-1633392;
Q62668-1:Slc14a2 (xeno); NbExp=6; IntAct=EBI-296723, EBI-1635608;
P11277:SPTB; NbExp=3; IntAct=EBI-296723, EBI-514908;
Q9UBB9:TFIP11; NbExp=4; IntAct=EBI-296723, EBI-1105213;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z266};
Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266};
Cytoplasmic side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm,
cytosol {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear
region {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546,
ECO:0000269|PubMed:21102408}. Golgi apparatus membrane
{ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane
{ECO:0000305|PubMed:25898167}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000305|PubMed:21102408}.
Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of
germ cells. {ECO:0000269|PubMed:19168546}.
-!- TISSUE SPECIFICITY: Expressed in male germ cells of adult testis
(at protein level). {ECO:0000269|PubMed:19168546}.
-!- DEVELOPMENTAL STAGE: Expressed in germ cells of 22-week prenatal
testis. {ECO:0000269|PubMed:19168546}.
-!- PTM: Phosphorylated by CSNK1D/CK1 (By similarity). Phosphorylated
by PKD, phosphorylation controls SNAPIN protein stability.
{ECO:0000250, ECO:0000269|PubMed:18167355,
ECO:0000269|PubMed:21102408}.
-!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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EMBL; AF086837; AAD11417.1; -; mRNA.
EMBL; AK024555; BAB14927.1; -; mRNA.
EMBL; BT006753; AAP35399.1; -; mRNA.
EMBL; AL592150; CAI18797.1; -; Genomic_DNA.
EMBL; CH471121; EAW53288.1; -; Genomic_DNA.
EMBL; CH471121; EAW53289.1; -; Genomic_DNA.
EMBL; BC000761; AAH00761.1; -; mRNA.
EMBL; BC004494; AAH04494.1; -; mRNA.
CCDS; CCDS1049.1; -.
RefSeq; NP_036569.1; NM_012437.5.
UniGene; Hs.32018; -.
ProteinModelPortal; O95295; -.
BioGrid; 117101; 59.
CORUM; O95295; -.
IntAct; O95295; 79.
MINT; MINT-5002303; -.
STRING; 9606.ENSP00000357674; -.
TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
iPTMnet; O95295; -.
PhosphoSitePlus; O95295; -.
BioMuta; SNAPIN; -.
EPD; O95295; -.
MaxQB; O95295; -.
PaxDb; O95295; -.
PeptideAtlas; O95295; -.
PRIDE; O95295; -.
DNASU; 23557; -.
Ensembl; ENST00000368685; ENSP00000357674; ENSG00000143553.
GeneID; 23557; -.
KEGG; hsa:23557; -.
UCSC; uc001fcq.5; human.
CTD; 23557; -.
DisGeNET; 23557; -.
EuPathDB; HostDB:ENSG00000143553.10; -.
GeneCards; SNAPIN; -.
HGNC; HGNC:17145; SNAPIN.
HPA; HPA046974; -.
MIM; 607007; gene.
neXtProt; NX_O95295; -.
OpenTargets; ENSG00000143553; -.
PharmGKB; PA162404012; -.
eggNOG; ENOG410J16C; Eukaryota.
eggNOG; ENOG4111JM9; LUCA.
GeneTree; ENSGT00390000008274; -.
HOGENOM; HOG000253926; -.
HOVERGEN; HBG056744; -.
InParanoid; O95295; -.
KO; K20002; -.
OMA; INEHQKV; -.
OrthoDB; EOG091G0WH1; -.
PhylomeDB; O95295; -.
TreeFam; TF319577; -.
Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
SIGNOR; O95295; -.
GeneWiki; SNAPAP; -.
GenomeRNAi; 23557; -.
PRO; PR:O95295; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143553; -.
CleanEx; HS_SNAPIN; -.
Genevisible; O95295; HS.
GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
GO; GO:0099078; C:BORC complex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0000149; F:SNARE binding; IDA:MGI.
GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
GO; GO:0034629; P:cellular protein complex localization; IEA:Ensembl.
GO; GO:0008333; P:endosome to lysosome transport; IGI:MGI.
GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
GO; GO:1902774; P:late endosome to lysosome transport; IEA:Ensembl.
GO; GO:0007042; P:lysosomal lumen acidification; IEA:Ensembl.
GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
GO; GO:0007269; P:neurotransmitter secretion; TAS:ProtInc.
GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; TAS:ParkinsonsUK-UCL.
GO; GO:0051604; P:protein maturation; IEA:Ensembl.
GO; GO:0043393; P:regulation of protein binding; IMP:ParkinsonsUK-UCL.
GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:MGI.
GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
GO; GO:0016188; P:synaptic vesicle maturation; IEA:Ensembl.
GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
GO; GO:0072553; P:terminal button organization; IEA:Ensembl.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR017246; Snapin.
InterPro; IPR028119; Snapin/Pallidin/Snn1.
PANTHER; PTHR31305; PTHR31305; 1.
Pfam; PF14712; Snapin_Pallidin; 1.
PIRSF; PIRSF037631; Snapin; 1.
1: Evidence at protein level;
Acetylation; Cell junction; Coiled coil; Complete proteome; Cytoplasm;
Cytoplasmic vesicle; Exocytosis; Golgi apparatus;
Host-virus interaction; Lysosome; Membrane; Phosphoprotein;
Polymorphism; Reference proteome; Synapse.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378}.
CHAIN 2 136 SNARE-associated protein Snapin.
/FTId=PRO_0000097556.
REGION 83 136 Interaction with TOR1A.
COILED 37 126 {ECO:0000255}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:22814378}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 14 14 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 50 50 Phosphoserine; by PKA.
{ECO:0000250|UniProtKB:Q9Z266}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 129 129 Phosphotyrosine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
VARIANT 112 112 S -> C (in dbSNP:rs1802461).
/FTId=VAR_017423.
SEQUENCE 136 AA; 14874 MW; 3EA402AC53C81FFF CRC64;
MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
RAMLDSGIYP PGSPGK


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