SNAPN_HUMAN
ID SNAPN_HUMAN Reviewed; 136 AA.
AC O95295; D3DV56; Q5SXU8;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=SNARE-associated protein Snapin;
DE AltName: Full=Biogenesis of lysosome-related organelles complex 1 subunit 7;
DE Short=BLOC-1 subunit 7;
DE AltName: Full=Synaptosomal-associated protein 25-binding protein;
DE Short=SNAP-associated protein;
GN Name=SNAPIN; Synonyms=BLOC1S7, SNAP25BP, SNAPAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10195194; DOI=10.1038/5673;
RA Ilardi J.M., Mochida S., Sheng Z.-H.;
RT "Snapin: a SNARE-associated protein implicated in synaptic transmission.";
RL Nat. Neurosci. 2:119-124(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Adipose tissue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung carcinoma, and Melanoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH RGS7.
RX PubMed=12659861; DOI=10.1016/s0006-291x(03)00400-5;
RA Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.;
RT "Snapin interacts with the N-terminus of regulator of G protein signaling
RT 7.";
RL Biochem. Biophys. Res. Commun. 303:594-599(2003).
RN [8]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX.
RX PubMed=15102850; DOI=10.1074/jbc.m402513200;
RA Starcevic M., Dell'Angelica E.C.;
RT "Identification of snapin and three novel proteins (BLOS1, BLOS2, and
RT BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related
RT organelles complex-1 (BLOC-1).";
RL J. Biol. Chem. 279:28393-28401(2004).
RN [9]
RP INTERACTION WITH CNTRL.
RX PubMed=16213214; DOI=10.1016/j.cell.2005.07.027;
RA Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S.,
RA Guha M., Sillibourne J., Doxsey S.J.;
RT "Centriolin anchoring of exocyst and SNARE complexes at the midbody is
RT required for secretory-vesicle-mediated abscission.";
RL Cell 123:75-87(2005).
RN [10]
RP FUNCTION.
RX PubMed=17182842; DOI=10.1091/mbc.e06-12-1066;
RA Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C.,
RA Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C.,
RA Dell'Angelica E.C., Raposo G., Marks M.S.;
RT "BLOC-1 is required for cargo-specific sorting from vacuolar early
RT endosomes toward lysosome-related organelles.";
RL Mol. Biol. Cell 18:768-780(2007).
RN [11]
RP FUNCTION IN VESICLE RECYCLING, INTERACTION WITH TOR1A, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RX PubMed=18167355; DOI=10.1074/jbc.m704097200;
RA Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.;
RT "The dystonia-associated protein torsinA modulates synaptic vesicle
RT recycling.";
RL J. Biol. Chem. 283:7568-7579(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [14]
RP SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE SPECIFICITY,
RP AND DEVELOPMENTAL STAGE.
RX PubMed=19168546; DOI=10.1093/molehr/gap004;
RA Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C.,
RA Kupryjanczyk J., Jaruzelska J.;
RT "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins
RT in human male germ cells.";
RL Mol. Hum. Reprod. 15:173-179(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-10; THR-14 AND SER-133, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [18]
RP INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
RX PubMed=21102408; DOI=10.1038/emboj.2010.285;
RA Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.;
RT "CSN complex controls the stability of selected synaptic proteins via a
RT torsinA-dependent process.";
RL EMBO J. 30:181-193(2011).
RN [19]
RP INTERACTION WITH HHV-5 PROTEIN UL70 (MICROBIAL INFECTION).
RX PubMed=21917956; DOI=10.1128/jvi.05357-11;
RA Shen A., Lei J., Yang E., Pei Y., Chen Y.C., Gong H., Xiao G., Liu F.;
RT "Human cytomegalovirus primase UL70 specifically interacts with cellular
RT factor Snapin.";
RL J. Virol. 85:11732-11741(2011).
RN [20]
RP IDENTIFICATION IN THE BLOC-1 COMPLEX, AND COMPOSITION OF THE BLOC-1
RP COMPLEX.
RX PubMed=22203680; DOI=10.1074/jbc.m111.325746;
RA Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C.,
RA Bonifacino J.S., Hurley J.H.;
RT "Assembly and architecture of biogenesis of lysosome-related organelles
RT complex-1 (BLOC-1).";
RL J. Biol. Chem. 287:5882-5890(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-14; SER-126 AND SER-133, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP FUNCTION, IDENTIFICATION OF THE BORC COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=25898167; DOI=10.1016/j.devcel.2015.02.011;
RA Pu J., Schindler C., Jia R., Jarnik M., Backlund P., Bonifacino J.S.;
RT "BORC, a multisubunit complex that regulates lysosome positioning.";
RL Dev. Cell 33:176-188(2015).
CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is required
CC for normal biogenesis of lysosome-related organelles (LRO), such as
CC platelet dense granules and melanosomes. In concert with the AP-3
CC complex, the BLOC-1 complex is required to target membrane protein
CC cargos into vesicles assembled at cell bodies for delivery into
CC neurites and nerve terminals. The BLOC-1 complex, in association with
CC SNARE proteins, is also proposed to be involved in neurite extension.
CC Plays a role in intracellular vesicle trafficking and synaptic vesicle
CC recycling. May modulate a step between vesicle priming, fusion and
CC calcium-dependent neurotransmitter release through its ability to
CC potentiate the interaction of synaptotagmin with the SNAREs and the
CC plasma-membrane-associated protein SNAP25. Its phosphorylation state
CC influences exocytotic protein interactions and may regulate synaptic
CC vesicle exocytosis. May also have a role in the mechanisms of SNARE-
CC mediated membrane fusion in non-neuronal cells (PubMed:17182842,
CC PubMed:18167355). As part of the BORC complex may play a role in
CC lysosomes movement and localization at the cell periphery. Associated
CC with the cytosolic face of lysosomes, the BORC complex may recruit
CC ARL8B and couple lysosomes to microtubule plus-end-directed kinesin
CC motor (PubMed:25898167). {ECO:0000269|PubMed:17182842,
CC ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:25898167}.
CC -!- SUBUNIT: Component of the biogenesis of lysosome-related organelles
CC complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4,
CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed
CC of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6,
CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with
CC the AP-3 protein complex and membrane protein cargos (PubMed:15102850,
CC PubMed:22203680). Component of the BLOC-one-related complex (BORC)
CC which is composed of BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8,
CC KXD1 and SNAPIN (PubMed:25898167). Associates with the SNARE complex.
CC Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2 and
CC SYT1. Interacts with SNAP25; the interaction with SNAP25 is increased
CC by its phosphorylation. Interacts with CNTRL, NANOS1, PUM2 and RGS7
CC (PubMed:12659861, PubMed:16213214, PubMed:19168546). Interacts with
CC TOR1A; the interaction is direct and associates SNAPIN with the CSN
CC complex (PubMed:18167355, PubMed:21102408).
CC {ECO:0000269|PubMed:12659861, ECO:0000269|PubMed:15102850,
CC ECO:0000269|PubMed:16213214, ECO:0000269|PubMed:18167355,
CC ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408,
CC ECO:0000269|PubMed:22203680, ECO:0000269|PubMed:25898167}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 protein UL70. {ECO:0000269|PubMed:21917956}.
CC -!- INTERACTION:
CC O95295; Q9NYB9-2: ABI2; NbExp=5; IntAct=EBI-296723, EBI-11096309;
CC O95295; Q8N9N5-2: BANP; NbExp=3; IntAct=EBI-296723, EBI-11524452;
CC O95295; Q12934-2: BFSP1; NbExp=3; IntAct=EBI-296723, EBI-12123320;
CC O95295; Q13515: BFSP2; NbExp=3; IntAct=EBI-296723, EBI-10229433;
CC O95295; P78537: BLOC1S1; NbExp=6; IntAct=EBI-296723, EBI-348630;
CC O95295; Q6QNY1: BLOC1S2; NbExp=10; IntAct=EBI-296723, EBI-465872;
CC O95295; A1L168: C20orf202; NbExp=3; IntAct=EBI-296723, EBI-18396958;
CC O95295; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-296723, EBI-10171570;
CC O95295; P51946: CCNH; NbExp=3; IntAct=EBI-296723, EBI-741406;
CC O95295; Q8IV53: DENND1C; NbExp=3; IntAct=EBI-296723, EBI-2871584;
CC O95295; Q96EV8: DTNBP1; NbExp=7; IntAct=EBI-296723, EBI-465804;
CC O95295; Q8IYW4: ENTHD1; NbExp=3; IntAct=EBI-296723, EBI-20842218;
CC O95295; Q9UPT5-1: EXOC7; NbExp=3; IntAct=EBI-296723, EBI-6251402;
CC O95295; A1L4K1: FSD2; NbExp=3; IntAct=EBI-296723, EBI-5661036;
CC O95295; Q70UQ0-4: IKBIP; NbExp=4; IntAct=EBI-296723, EBI-12190633;
CC O95295; Q2T9L4: INSYN1; NbExp=3; IntAct=EBI-296723, EBI-4311436;
CC O95295; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-296723, EBI-2556193;
CC O95295; P19012: KRT15; NbExp=3; IntAct=EBI-296723, EBI-739566;
CC O95295; P08779: KRT16; NbExp=3; IntAct=EBI-296723, EBI-356410;
CC O95295; P08727: KRT19; NbExp=3; IntAct=EBI-296723, EBI-742756;
CC O95295; P35900: KRT20; NbExp=3; IntAct=EBI-296723, EBI-742094;
CC O95295; Q2M2I5: KRT24; NbExp=6; IntAct=EBI-296723, EBI-2952736;
CC O95295; Q7Z3Y9: KRT26; NbExp=3; IntAct=EBI-296723, EBI-12084444;
CC O95295; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-296723, EBI-3044087;
CC O95295; P20700: LMNB1; NbExp=3; IntAct=EBI-296723, EBI-968218;
CC O95295; Q5S007: LRRK2; NbExp=5; IntAct=EBI-296723, EBI-5323863;
CC O95295; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-296723, EBI-10172876;
CC O95295; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-296723, EBI-744782;
CC O95295; Q9H1M0: NUP62CL; NbExp=3; IntAct=EBI-296723, EBI-751933;
CC O95295; P49585: PCYT1A; NbExp=3; IntAct=EBI-296723, EBI-2563309;
CC O95295; Q5JTB6: PLAC9; NbExp=3; IntAct=EBI-296723, EBI-3923605;
CC O95295; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-296723, EBI-14093916;
CC O95295; Q96BD8: SKA1; NbExp=5; IntAct=EBI-296723, EBI-741854;
CC O95295; Q15849-1: SLC14A2; NbExp=5; IntAct=EBI-296723, EBI-1633392;
CC O95295; P11277: SPTB; NbExp=3; IntAct=EBI-296723, EBI-514908;
CC O95295; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-296723, EBI-1105213;
CC O95295; P07951-2: TPM2; NbExp=3; IntAct=EBI-296723, EBI-10977815;
CC O95295; P06753: TPM3; NbExp=3; IntAct=EBI-296723, EBI-355607;
CC O95295; P67936: TPM4; NbExp=3; IntAct=EBI-296723, EBI-1642100;
CC O95295; Q99816: TSG101; NbExp=3; IntAct=EBI-296723, EBI-346882;
CC O95295; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-296723, EBI-712969;
CC O95295; Q62668-1: Slc14a2; Xeno; NbExp=6; IntAct=EBI-296723, EBI-1635608;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:Q9Z266};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z266}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Z266}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546,
CC ECO:0000269|PubMed:21102408}. Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9Z266}. Lysosome membrane
CC {ECO:0000305|PubMed:25898167}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000305|PubMed:21102408}.
CC Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ
CC cells. {ECO:0000269|PubMed:19168546}.
CC -!- TISSUE SPECIFICITY: Expressed in male germ cells of adult testis (at
CC protein level). {ECO:0000269|PubMed:19168546}.
CC -!- DEVELOPMENTAL STAGE: Expressed in germ cells of 22-week prenatal
CC testis. {ECO:0000269|PubMed:19168546}.
CC -!- PTM: Phosphorylated by CSNK1D/CK1 (By similarity). Phosphorylated by
CC PKD, phosphorylation controls SNAPIN protein stability. {ECO:0000250,
CC ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:21102408}.
CC -!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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DR EMBL; AF086837; AAD11417.1; -; mRNA.
DR EMBL; AK024555; BAB14927.1; -; mRNA.
DR EMBL; BT006753; AAP35399.1; -; mRNA.
DR EMBL; AL592150; CAI18797.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53288.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW53289.1; -; Genomic_DNA.
DR EMBL; BC000761; AAH00761.1; -; mRNA.
DR EMBL; BC004494; AAH04494.1; -; mRNA.
DR CCDS; CCDS1049.1; -.
DR RefSeq; NP_036569.1; NM_012437.5.
DR AlphaFoldDB; O95295; -.
DR SMR; O95295; -.
DR BioGRID; 117101; 151.
DR ComplexPortal; CPX-1910; BLOC-1 complex.
DR ComplexPortal; CPX-5029; BORC complex.
DR CORUM; O95295; -.
DR IntAct; O95295; 121.
DR MINT; O95295; -.
DR STRING; 9606.ENSP00000357674; -.
DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family.
DR GlyGen; O95295; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95295; -.
DR PhosphoSitePlus; O95295; -.
DR BioMuta; SNAPIN; -.
DR EPD; O95295; -.
DR jPOST; O95295; -.
DR MassIVE; O95295; -.
DR MaxQB; O95295; -.
DR PaxDb; O95295; -.
DR PeptideAtlas; O95295; -.
DR PRIDE; O95295; -.
DR ProteomicsDB; 50792; -.
DR ABCD; O95295; 1 sequenced antibody.
DR Antibodypedia; 34134; 136 antibodies from 29 providers.
DR DNASU; 23557; -.
DR Ensembl; ENST00000368685.6; ENSP00000357674.5; ENSG00000143553.11.
DR GeneID; 23557; -.
DR KEGG; hsa:23557; -.
DR MANE-Select; ENST00000368685.6; ENSP00000357674.5; NM_012437.6; NP_036569.1.
DR UCSC; uc001fcq.5; human.
DR CTD; 23557; -.
DR DisGeNET; 23557; -.
DR GeneCards; SNAPIN; -.
DR HGNC; HGNC:17145; SNAPIN.
DR HPA; ENSG00000143553; Low tissue specificity.
DR MIM; 607007; gene.
DR neXtProt; NX_O95295; -.
DR OpenTargets; ENSG00000143553; -.
DR PharmGKB; PA162404012; -.
DR VEuPathDB; HostDB:ENSG00000143553; -.
DR eggNOG; ENOG502S07W; Eukaryota.
DR GeneTree; ENSGT00390000008274; -.
DR HOGENOM; CLU_124640_1_0_1; -.
DR InParanoid; O95295; -.
DR OMA; QLDTHVH; -.
DR OrthoDB; 1532513at2759; -.
DR PhylomeDB; O95295; -.
DR TreeFam; TF319577; -.
DR PathwayCommons; O95295; -.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; O95295; -.
DR SIGNOR; O95295; -.
DR BioGRID-ORCS; 23557; 107 hits in 1078 CRISPR screens.
DR ChiTaRS; SNAPIN; human.
DR GeneWiki; SNAPAP; -.
DR GenomeRNAi; 23557; -.
DR Pharos; O95295; Tbio.
DR PRO; PR:O95295; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O95295; protein.
DR Bgee; ENSG00000143553; Expressed in oocyte and 181 other tissues.
DR Genevisible; O95295; HS.
DR GO; GO:0001669; C:acrosomal vesicle; IEA:Ensembl.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC.
DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB.
DR GO; GO:0099078; C:BORC complex; IDA:UniProtKB.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002177; C:manchette; IEA:Ensembl.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:UniProtKB.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; IDA:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; ISS:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IEA:Ensembl.
DR GO; GO:0008333; P:endosome to lysosome transport; IGI:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc.
DR GO; GO:1902774; P:late endosome to lysosome transport; IEA:Ensembl.
DR GO; GO:0007042; P:lysosomal lumen acidification; IEA:Ensembl.
DR GO; GO:0032418; P:lysosome localization; IMP:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IBA:GO_Central.
DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
DR GO; GO:0070050; P:neuron cellular homeostasis; IEA:Ensembl.
DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR GO; GO:0007269; P:neurotransmitter secretion; TAS:ProtInc.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; TAS:ParkinsonsUK-UCL.
DR GO; GO:0051604; P:protein maturation; IEA:Ensembl.
DR GO; GO:0031503; P:protein-containing complex localization; IEA:Ensembl.
DR GO; GO:0051036; P:regulation of endosome size; IC:ComplexPortal.
DR GO; GO:0062196; P:regulation of lysosome size; IC:ComplexPortal.
DR GO; GO:0043393; P:regulation of protein binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IBA:GO_Central.
DR GO; GO:0008090; P:retrograde axonal transport; IEA:Ensembl.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IEA:Ensembl.
DR GO; GO:0016188; P:synaptic vesicle maturation; IEA:Ensembl.
DR GO; GO:0048489; P:synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0072553; P:terminal button organization; IEA:Ensembl.
DR InterPro; IPR017246; Snapin.
DR InterPro; IPR028119; Snapin/Pallidin/Snn1.
DR PANTHER; PTHR31305; PTHR31305; 1.
DR Pfam; PF14712; Snapin_Pallidin; 1.
DR PIRSF; PIRSF037631; Snapin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Coiled coil; Cytoplasm; Cytoplasmic vesicle; Exocytosis;
KW Golgi apparatus; Host-virus interaction; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT CHAIN 2..136
FT /note="SNARE-associated protein Snapin"
FT /id="PRO_0000097556"
FT REGION 83..136
FT /note="Interaction with TOR1A"
FT COILED 37..126
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 50
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q9Z266"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 112
FT /note="S -> C (in dbSNP:rs1802461)"
FT /id="VAR_017423"
SQ SEQUENCE 136 AA; 14874 MW; 3EA402AC53C81FFF CRC64;
MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
RAMLDSGIYP PGSPGK
