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-MAY-2011, entry version 87. DE RecName: Full=SNARE-associated protein Snapin; DE AltName: Full=Synaptosomal-associated protein 25-binding protein; DE Short=SNAP-associated protein; GN Name=SNAPIN; Synonyms=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 MEDLINE=99211098; 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 BLOC1 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 CEP110. 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS RP SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=17287340; DOI=10.1073/pnas.0611217104; RA Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; RT "Global proteomic profiling of phosphopeptides using electron transfer RT dissociation tandem mass spectrometry."; RL Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND MASS RP SPECTROMETRY. 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, PHOSPHORYLATION [LARGE RP SCALE ANALYSIS] AT THR-14 AND SER-133, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, AND RP MASS SPECTROMETRY. 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 [14] 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). CC -!- FUNCTION: May modulate a step between vesicle priming, fusion and CC calcium-dependent neurotransmitter release by potentiating the CC interaction of synaptotagmins 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 cells CC (By similarity). CC -!- SUBUNIT: Associates with the SNARE complex. Interacts with SNAP23, CC SNAP25 and STX4A but not with STX1A, VAMP2 and SYT1. CC Phosphorylation increases its interaction with SNAP25 (By CC similarity). Interacts with RGS7. Component of the biogenesis of CC lysosome-related organelles (BLOC-1) complex which is required for CC normal biogenesis of specialized organelles of the endosomal- CC lysosomal system. Interacts with CEP110. CC -!- INTERACTION: CC Q6QNY1:BLOC1S2; NbExp=1; IntAct=EBI-296723, EBI-465872; CC Q6QNY0:BLOC1S3; NbExp=1; IntAct=EBI-296723, EBI-465930; CC Q96EV8:DTNBP1; NbExp=1; IntAct=EBI-296723, EBI-465804; CC Q9UL45:PLDN; NbExp=1; IntAct=EBI-296723, EBI-465781; CC Q15849-1:SLC14A2; NbExp=4; IntAct=EBI-296723, EBI-1633392; CC Q62668-1:Slc14a2 (xeno); NbExp=2; IntAct=EBI-296723, EBI-1635608; 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 Note=May be cytoplasmic and peripheral membrane bound or anchored CC to the vesicular membrane through an N-terminal signal anchor (By CC similarity). 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 IPI; IPI00018331; -. DR RefSeq; NP_036569.1; NM_012437.4. DR UniGene; Hs.32018; -. DR ProteinModelPortal; O95295; -. DR IntAct; O95295; 44. DR MINT; MINT-5002303; -. DR STRING; O95295; -. DR TCDB; 1.F.1.1.1; synaptosomal vesicle fusion pore (SVF-Pore) family. DR PhosphoSite; O95295; -. DR PeptideAtlas; O95295; -. DR PRIDE; O95295; -. DR Ensembl; ENST00000368685; ENSP00000357674; ENSG00000143553. DR GeneID; 23557; -. DR KEGG; hsa:23557; -. DR UCSC; uc001fcq.1; human. DR CTD; 23557; -. DR GeneCards; GC01P124994; -. DR H-InvDB; HIX0001087; -. DR HGNC; HGNC:17145; SNAPIN. DR MIM; 607007; gene. DR neXtProt; NX_O95295; -. DR PharmGKB; PA162404012; -. DR GeneTree; ENSGT00390000008274; -. DR HOGENOM; HBG717464; -. DR HOVERGEN; HBG056744; -. DR InParanoid; O95295; -. DR OMA; CRINEHQ; -. DR OrthoDB; EOG4X6C9S; -. DR PhylomeDB; O95295; -. DR Reactome; REACT_11123; Membrane Trafficking. DR NextBio; 46130; -. DR ArrayExpress; O95295; -. DR Bgee; O95295; -. DR CleanEx; HS_SNAPIN; -. DR Genevestigator; O95295; -. DR GermOnline; ENSG00000143553; Homo sapiens. DR GO; GO:0031083; C:BLOC-1 complex; IDA:UniProtKB. DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0019717; C:synaptosome; IDA:MGI. DR GO; GO:0000149; F:SNARE binding; IDA:MGI. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0016079; P:synaptic vesicle exocytosis; IDA:MGI. DR InterPro; IPR017246; Snapin. DR PIRSF; PIRSF037631; Snapin; 1. PE 1: Evidence at protein level; KW Acetylation; Cell junction; Coiled coil; Complete proteome; Cytoplasm; KW Cytoplasmic vesicle; Exocytosis; Membrane; Phosphoprotein; KW Polymorphism; 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 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 //