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 16-APR-2014, entry version 115. 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 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 [12] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR RP METHIONINE [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 [13] 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 [14] 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 [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT SER-10; THR-14 AND SER-133, AND IDENTIFICATION BY RP MASS 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 [16] 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 [17] 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 [18] 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 [19] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND IDENTIFICATION BY RP MASS 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). 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. May modulate a step between vesicle priming, fusion CC and calcium-dependent neurotransmitter release through its ability CC to potentiate the interaction of synaptotagmin with the SNAREs and CC the plasma-membrane-associated protein SNAP25. Its phosphorylation CC state 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. 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 (By similarity). CC Component of the biogenesis of lysosome-related organelles complex CC 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer CC composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, CC BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 CC complex associates with the AP-3 protein complex and membrane CC protein cargos. Associates with the SNARE complex. Interacts with CC CNTRL, NANOS1, PUM2 and RGS7. Interacts with human CC cytomegalovirus/HHV-5 protein UL70. 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 (By similarity). Membrane; CC Peripheral membrane protein; Cytoplasmic side (By similarity). CC Cytoplasmic vesicle membrane; Peripheral membrane protein; CC Cytoplasmic side (By similarity). Cytoplasmic vesicle, secretory CC vesicle, synaptic vesicle membrane; Peripheral membrane protein; CC Cytoplasmic side (Potential). Cell junction, synapse, synaptosome. CC Cytoplasm, perinuclear region. Golgi apparatus membrane (By CC similarity). Note=May be cytoplasmic and peripheral membrane bound CC or anchored to the vesicular membrane through an N-terminal signal CC anchor (By similarity). Colocalizes with NANOS1 and PUM2 in the CC perinuclear region of germ cells. CC -!- TISSUE SPECIFICITY: Expressed in male germ cells of adult testis CC (at protein level). CC -!- DEVELOPMENTAL STAGE: Expressed in germ cells of 22-week prenatal CC testis. CC -!- PTM: Phosphorylated by CSNK1D/CK1 (By similarity). CC -!- SIMILARITY: Belongs to the SNAPIN family. 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 RefSeq; NP_036569.1; NM_012437.5. DR UniGene; Hs.32018; -. DR ProteinModelPortal; O95295; -. DR BioGrid; 117101; 32. DR IntAct; O95295; 66. DR MINT; MINT-5002303; -. DR STRING; 9606.ENSP00000357674; -. DR TCDB; 1.F.1.1.1; the synaptosomal vesicle fusion pore (svf-pore) family. DR PhosphoSite; 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.4; human. DR CTD; 23557; -. DR GeneCards; GC01P153631; -. DR HGNC; HGNC:17145; SNAPIN. DR HPA; HPA046974; -. DR MIM; 607007; gene. DR neXtProt; NX_O95295; -. DR PharmGKB; PA162404012; -. DR eggNOG; NOG83669; -. DR HOGENOM; HOG000253926; -. DR HOVERGEN; HBG056744; -. DR InParanoid; O95295; -. DR OMA; ENTENFC; -. DR OrthoDB; EOG7SXW5D; -. DR PhylomeDB; O95295; -. DR TreeFam; TF319577; -. DR Reactome; REACT_11123; Membrane Trafficking. DR GeneWiki; SNAPAP; -. DR GenomeRNAi; 23557; -. DR NextBio; 46130; -. DR PRO; PR:O95295; -. DR Bgee; O95295; -. DR CleanEx; HS_SNAPIN; -. DR Genevestigator; O95295; -. 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:0043005; C:neuron projection; 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:0045202; C:synapse; IDA:MGI. DR GO; GO:0008021; C:synaptic vesicle; TAS:ProtInc. 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 axon cargo transport; ISS:UniProtKB. DR GO; GO:0048490; P:anterograde synaptic vesicle transport; ISS:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0032438; P:melanosome organization; NAS:UniProtKB. DR GO; GO:0031175; P:neuron projection development; ISS:UniProtKB. DR GO; GO:0007269; P:neurotransmitter secretion; TAS:ProtInc. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:MGI. DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic membrane; IEA:Ensembl. DR GO; GO:0016188; P:synaptic vesicle maturation; IEA:Ensembl. 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; Synaptosome. FT INIT_MET 1 1 Removed. FT CHAIN 2 136 SNARE-associated protein Snapin. FT /FTId=PRO_0000097556. FT COILED 37 126 Potential. FT MOD_RES 2 2 N-acetylalanine. FT MOD_RES 10 10 Phosphoserine. FT MOD_RES 14 14 Phosphothreonine. FT MOD_RES 50 50 Phosphoserine; by PKA (By similarity). FT MOD_RES 129 129 Phosphotyrosine. FT MOD_RES 133 133 Phosphoserine. 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 //