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 06-JUL-2016, entry version 136. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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 RT 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 RT 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT signaling 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- RT related 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., RA Theos A.C., 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 RP BY 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 RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE RP SPECIFICITY, 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 RT proteins 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 RP SCALE ANALYSIS] AT SER-10; THR-14 AND SER-133, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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., RA Buerckstuemmer T., 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 RT a torsinA-dependent process."; RL EMBO J. 30:181-193(2011). RN [19] RP INTERACTION WITH HHV-5 PROTEIN UL70. 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 RT cellular 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., RA Steven A.C., Bonifacino J.S., Hurley J.H.; RT "Assembly and architecture of biogenesis of lysosome-related RT organelles 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 RP SPECTROMETRY [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., RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., RA Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N- RT terminal 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, RP AND 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). CC -!- FUNCTION: Component of the BLOC-1 complex, a complex that is CC required for normal biogenesis of lysosome-related organelles CC (LRO), such as platelet dense granules and melanosomes. In concert CC with the AP-3 complex, the BLOC-1 complex is required to target CC membrane protein cargos into vesicles assembled at cell bodies for CC delivery into neurites and nerve terminals. The BLOC-1 complex, in CC association with SNARE proteins, is also proposed to be involved CC in neurite extension. Plays a role in intracellular vesicle CC trafficking and synaptic vesicle recycling. May modulate a step CC between vesicle priming, fusion and calcium-dependent CC neurotransmitter release through its ability to potentiate the CC interaction of synaptotagmin with the SNAREs and the plasma- CC membrane-associated protein SNAP25. Its phosphorylation state CC influences exocytotic protein interactions and may regulate CC synaptic vesicle exocytosis. May also have a role in the CC mechanisms of SNARE-mediated membrane fusion in non-neuronal CC cells. {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18167355}. CC -!- SUBUNIT: Interacts with CSNK1D, SNAP23 and STX4A but not with CC STX1A, VAMP2 and SYT1. Interacts with SNAP25; the interaction with CC SNAP25 is increased by its phosphorylation. Component of the CC biogenesis of lysosome-related organelles complex 1 (BLOC-1) CC composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy CC each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, CC DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates CC with the AP-3 protein complex and membrane protein cargos. CC Associates with the SNARE complex. Interacts with CNTRL, NANOS1, CC PUM2 and RGS7. Interacts with TOR1A; the interaction is direct and CC associates SNAPIN with the CSN complex. Interacts with human CC cytomegalovirus/HHV-5 protein UL70. {ECO:0000269|PubMed:12659861, CC ECO:0000269|PubMed:15102850, ECO:0000269|PubMed:16213214, CC ECO:0000269|PubMed:18167355, ECO:0000269|PubMed:19168546, CC ECO:0000269|PubMed:21102408, ECO:0000269|PubMed:21917956, CC ECO:0000269|PubMed:22203680}. CC -!- INTERACTION: CC Q6QNY1:BLOC1S2; NbExp=7; IntAct=EBI-296723, EBI-465872; CC Q9UL45:BLOC1S6; NbExp=2; IntAct=EBI-296723, EBI-465781; CC Q96EV8:DTNBP1; NbExp=4; IntAct=EBI-296723, EBI-465804; CC O75923:DYSF; NbExp=3; IntAct=EBI-296723, EBI-2799016; CC Q5S007:LRRK2; NbExp=5; IntAct=EBI-296723, EBI-5323863; CC Q15849-1:SLC14A2; NbExp=5; IntAct=EBI-296723, EBI-1633392; CC Q62668-1:Slc14a2 (xeno); NbExp=6; IntAct=EBI-296723, EBI-1635608; CC P11277:SPTB; NbExp=3; IntAct=EBI-296723, EBI-514908; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle membrane CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle membrane {ECO:0000305}; Peripheral CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. CC Cytoplasm, perinuclear region {ECO:0000269|PubMed:18167355, CC ECO:0000269|PubMed:19168546, ECO:0000269|PubMed:21102408}. Golgi CC apparatus membrane {ECO:0000250}. Cytoplasmic vesicle, secretory CC vesicle {ECO:0000250}. Note=May be cytoplasmic and peripheral CC membrane bound or anchored to the vesicular membrane through an N- CC terminal signal anchor (By similarity). Colocalizes with NANOS1 CC and PUM2 in the perinuclear region of germ cells. {ECO:0000250}. CC -!- TISSUE SPECIFICITY: Expressed in male germ cells of adult testis CC (at 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 CC by PKD, phosphorylation controls SNAPIN protein stability. CC {ECO:0000250, ECO:0000269|PubMed:18167355, CC ECO:0000269|PubMed:21102408}. CC -!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 UniGene; Hs.32018; -. DR ProteinModelPortal; O95295; -. DR BioGrid; 117101; 50. DR IntAct; O95295; 69. DR MINT; MINT-5002303; -. DR STRING; 9606.ENSP00000357674; -. DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family. DR iPTMnet; O95295; -. DR PhosphoSite; O95295; -. DR BioMuta; SNAPIN; -. DR EPD; O95295; -. DR MaxQB; O95295; -. DR PaxDb; O95295; -. DR PeptideAtlas; O95295; -. DR PRIDE; O95295; -. DR DNASU; 23557; -. DR Ensembl; ENST00000368685; ENSP00000357674; ENSG00000143553. DR GeneID; 23557; -. DR KEGG; hsa:23557; -. DR UCSC; uc001fcq.5; human. DR CTD; 23557; -. DR GeneCards; SNAPIN; -. DR HGNC; HGNC:17145; SNAPIN. DR HPA; HPA046974; -. DR MIM; 607007; gene. DR neXtProt; NX_O95295; -. DR PharmGKB; PA162404012; -. DR eggNOG; ENOG410J16C; Eukaryota. DR eggNOG; ENOG4111JM9; LUCA. DR GeneTree; ENSGT00390000008274; -. DR HOGENOM; HOG000253926; -. DR HOVERGEN; HBG056744; -. DR InParanoid; O95295; -. DR KO; K20002; -. DR OMA; INEHQKV; -. DR OrthoDB; EOG7SXW5D; -. DR PhylomeDB; O95295; -. DR TreeFam; TF319577; -. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR SIGNOR; O95295; -. DR GeneWiki; SNAPAP; -. DR GenomeRNAi; 23557; -. DR PRO; PR:O95295; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; O95295; -. DR CleanEx; HS_SNAPIN; -. DR Genevisible; O95295; HS. DR GO; GO:1904115; C:axon cytoplasm; IEA:GOC. DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005730; C:nucleolus; IDA:HPA. 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:0032438; P:melanosome organization; NAS:UniProtKB. DR GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0007269; P:neurotransmitter secretion; TAS:ProtInc. DR GO; GO:1902824; P:positive regulation of late endosome to lysosome transport; TAS:ParkinsonsUK-UCL. DR GO; GO:0043393; P:regulation of protein binding; IMP:ParkinsonsUK-UCL. 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 GO; GO:0016032; P:viral process; IEA:UniProtKB-KW. 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; Cell junction; Coiled coil; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Exocytosis; Golgi apparatus; KW Host-virus interaction; Membrane; Phosphoprotein; Polymorphism; KW Reference proteome; Synapse. FT INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:22814378}. FT CHAIN 2 136 SNARE-associated protein Snapin. FT /FTId=PRO_0000097556. FT REGION 83 136 Interaction with TOR1A. FT COILED 37 126 {ECO:0000255}. FT MOD_RES 2 2 N-acetylalanine. FT {ECO:0000244|PubMed:19413330, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:22814378}. FT MOD_RES 10 10 Phosphoserine. FT {ECO:0000244|PubMed:20068231}. FT MOD_RES 14 14 Phosphothreonine. FT {ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT MOD_RES 50 50 Phosphoserine; by PKA. {ECO:0000250}. FT MOD_RES 126 126 Phosphoserine. FT {ECO:0000244|PubMed:23186163}. FT MOD_RES 129 129 Phosphotyrosine. FT {ECO:0000244|PubMed:19690332}. FT MOD_RES 133 133 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:20068231, FT ECO:0000244|PubMed:23186163}. FT VARIANT 112 112 S -> C (in dbSNP:rs1802461). FT /FTId=VAR_017423. SQ SEQUENCE 136 AA; 14874 MW; 3EA402AC53C81FFF CRC64; MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK //