SNAPN_MOUSE
ID SNAPN_MOUSE Reviewed; 136 AA.
AC Q9Z266; Q3U8V4; Q922V7;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 161.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH SNAP25.
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] (ISOFORM 1).
RC STRAIN=C57BL/6J;
RC TISSUE=Bone marrow, Forelimb, Head, Liver, Pancreas, and Retina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Limb, and Mammary tumor;
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, TOPOLOGY, AND INTERACTION WITH
RP SNAP23 AND STX4A.
RX PubMed=12877659; DOI=10.1042/bj20030427;
RA Buxton P., Zhang X.-M., Walsh B., Sriratana A., Schenberg I., Manickam E.,
RA Rowe T.;
RT "Identification and characterization of Snapin as a ubiquitously expressed
RT SNARE-binding protein that interacts with SNAP23 in non-neuronal cells.";
RL Biochem. J. 375:433-440(2003).
RN [5]
RP PHOSPHORYLATION AT SER-50, INTERACTION WITH SNAP25, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF SER-42; SER-50 AND THR-63.
RX PubMed=11283605; DOI=10.1038/35070000;
RA Chheda M.G., Ashery U., Thakur P., Rettig J., Sheng Z.-H.;
RT "Phosphorylation of Snapin by PKA modulates its interaction with the SNARE
RT complex.";
RL Nat. Cell Biol. 3:331-338(2001).
RN [6]
RP REVIEW ON PHOSPHORYLATION.
RX PubMed=12887314; DOI=10.1042/bst0310824;
RA Evans G.J., Morgan A.;
RT "Regulation of the exocytotic machinery by cAMP-dependent protein kinase:
RT implications for presynaptic plasticity.";
RL Biochem. Soc. Trans. 31:824-827(2003).
RN [7]
RP PHOSPHORYLATION BY CSNK1D/CK1, SUBCELLULAR LOCATION, AND INTERACTION WITH
RP CSNK1D.
RX PubMed=17101137; DOI=10.1016/j.febslet.2006.10.068;
RA Wolff S., Stoeter M., Giamas G., Piesche M., Henne-Bruns D., Banting G.,
RA Knippschild U.;
RT "Casein kinase 1 delta (CK1delta) interacts with the SNARE associated
RT protein snapin.";
RL FEBS Lett. 580:6477-6484(2006).
RN [8]
RP FUNCTION.
RX PubMed=16760431; DOI=10.1091/mbc.e06-02-0103;
RA Salazar G., Craige B., Styers M.L., Newell-Litwa K.A., Doucette M.M.,
RA Wainer B.H., Falcon-Perez J.M., Dell'Angelica E.C., Peden A.A., Werner E.,
RA Faundez V.;
RT "BLOC-1 complex deficiency alters the targeting of adaptor protein complex-
RT 3 cargoes.";
RL Mol. Biol. Cell 17:4014-4026(2006).
RN [9]
RP TISSUE SPECIFICITY.
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP FUNCTION.
RX PubMed=19546860; DOI=10.1038/mp.2009.58;
RA Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R.,
RA Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C.,
RA Dell'Angelica E.C.;
RT "The dysbindin-containing complex (BLOC-1) in brain: developmental
RT regulation, interaction with SNARE proteins and role in neurite
RT outgrowth.";
RL Mol. Psychiatry 15:204-215(2010).
RN [12]
RP FUNCTION, AND ASSOCIATION WITH THE AP-3 COMPLEX.
RX PubMed=21998198; DOI=10.1091/mbc.e11-07-0592;
RA Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B.,
RA Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.;
RT "The schizophrenia susceptibility factor dysbindin and its associated
RT complex sort cargoes from cell bodies to the synapse.";
RL Mol. Biol. Cell 22:4854-4867(2011).
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:16760431,
CC PubMed:19546860, PubMed:21998198). As part of the BORC complex may play
CC a role in lysosomes movement and localization at the cell periphery.
CC Associated with the cytosolic face of lysosomes, the BORC complex may
CC recruit ARL8B and couple lysosomes to microtubule plus-end-directed
CC kinesin motor (By similarity). {ECO:0000250|UniProtKB:O95295,
CC ECO:0000269|PubMed:16760431, ECO:0000269|PubMed:19546860,
CC ECO:0000269|PubMed:21998198}.
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:21998198).
CC Component of the BLOC-one-related complex (BORC) which is composed of
CC BLOC1S1, BLOC1S2, BORCS5, BORCS6, BORCS7, BORCS8, KXD1 and SNAPIN (By
CC similarity). Associates with the SNARE complex. Interacts with CSNK1D,
CC SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1 (PubMed:12877659,
CC PubMed:17101137). Interacts with SNAP25; the interaction with SNAP25 is
CC increased by its phosphorylation (PubMed:10195194, PubMed:11283605).
CC Interacts with CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the
CC interaction is direct and associates SNAPIN with the CSN complex (By
CC similarity). {ECO:0000250|UniProtKB:O95295,
CC ECO:0000269|PubMed:10195194, ECO:0000269|PubMed:11283605,
CC ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:17101137,
CC ECO:0000269|PubMed:21998198}.
CC -!- INTERACTION:
CC Q9Z266; Q06486-2: Csnk1d; Xeno; NbExp=4; IntAct=EBI-6170320, EBI-7088890;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12877659};
CC Peripheral membrane protein {ECO:0000269|PubMed:12877659}; Cytoplasmic
CC side {ECO:0000269|PubMed:12877659}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:12877659}. Cytoplasm, perinuclear region
CC {ECO:0000269|PubMed:12877659}. Golgi apparatus membrane
CC {ECO:0000269|PubMed:17101137}. Lysosome membrane
CC {ECO:0000250|UniProtKB:O95295}. Cytoplasmic vesicle, secretory vesicle,
CC synaptic vesicle membrane {ECO:0000269|PubMed:11283605}.
CC Note=Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ
CC cells. {ECO:0000250|UniProtKB:O95295}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z266-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Z266-2; Sequence=VSP_009165, VSP_009166;
CC -!- TISSUE SPECIFICITY: Strongly expressed in heart, brain, testis, kidney
CC and liver; low expression in spleen, lung and skeletal muscle. In the
CC testis, expressed in the seminiferous tubules.
CC {ECO:0000269|PubMed:12877659, ECO:0000269|PubMed:19168546}.
CC -!- PTM: Phosphorylated by PKD, phosphorylation controls SNAPIN protein
CC stability (By similarity). Phosphorylated by CSNK1D/CK1. {ECO:0000250,
CC ECO:0000269|PubMed:11283605, ECO:0000269|PubMed:17101137}.
CC -!- SIMILARITY: Belongs to the SNAPIN family. {ECO:0000305}.
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DR EMBL; AF086838; AAD11418.1; -; mRNA.
DR EMBL; AK007458; BAB25049.1; -; mRNA.
DR EMBL; AK048007; BAC33212.1; -; mRNA.
DR EMBL; AK050151; BAC34095.1; -; mRNA.
DR EMBL; AK077840; BAC37029.1; -; mRNA.
DR EMBL; AK080718; BAC37991.1; -; mRNA.
DR EMBL; AK152057; BAE30913.1; -; mRNA.
DR EMBL; BC006744; AAH06744.1; -; mRNA.
DR EMBL; BC048691; AAH48691.1; -; mRNA.
DR CCDS; CCDS17531.1; -. [Q9Z266-1]
DR RefSeq; NP_598615.1; NM_133854.3. [Q9Z266-1]
DR AlphaFoldDB; Q9Z266; -.
DR SMR; Q9Z266; -.
DR BioGRID; 203363; 22.
DR ComplexPortal; CPX-1913; BLOC-1 complex.
DR ComplexPortal; CPX-5061; BORC complex.
DR CORUM; Q9Z266; -.
DR IntAct; Q9Z266; 5.
DR MINT; Q9Z266; -.
DR STRING; 10090.ENSMUSP00000122090; -.
DR iPTMnet; Q9Z266; -.
DR PhosphoSitePlus; Q9Z266; -.
DR EPD; Q9Z266; -.
DR MaxQB; Q9Z266; -.
DR PaxDb; Q9Z266; -.
DR PeptideAtlas; Q9Z266; -.
DR PRIDE; Q9Z266; -.
DR ProteomicsDB; 261384; -. [Q9Z266-1]
DR ProteomicsDB; 261385; -. [Q9Z266-2]
DR ABCD; Q9Z266; 1 sequenced antibody.
DR Antibodypedia; 34134; 136 antibodies from 29 providers.
DR DNASU; 20615; -.
DR Ensembl; ENSMUST00000149884; ENSMUSP00000122090; ENSMUSG00000001018. [Q9Z266-1]
DR GeneID; 20615; -.
DR KEGG; mmu:20615; -.
DR UCSC; uc008qck.2; mouse. [Q9Z266-1]
DR CTD; 23557; -.
DR MGI; MGI:1333745; Snapin.
DR VEuPathDB; HostDB:ENSMUSG00000001018; -.
DR eggNOG; ENOG502S07W; Eukaryota.
DR GeneTree; ENSGT00390000008274; -.
DR HOGENOM; CLU_124640_1_0_1; -.
DR InParanoid; Q9Z266; -.
DR OMA; QLDTHVH; -.
DR OrthoDB; 1532513at2759; -.
DR PhylomeDB; Q9Z266; -.
DR TreeFam; TF319577; -.
DR Reactome; R-MMU-432722; Golgi Associated Vesicle Biogenesis.
DR BioGRID-ORCS; 20615; 3 hits in 73 CRISPR screens.
DR ChiTaRS; Snapin; mouse.
DR PRO; PR:Q9Z266; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q9Z266; protein.
DR Bgee; ENSMUSG00000001018; Expressed in floor plate of midbrain and 258 other tissues.
DR ExpressionAtlas; Q9Z266; baseline and differential.
DR Genevisible; Q9Z266; MM.
DR GO; GO:0001669; C:acrosomal vesicle; IDA:MGI.
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:MGI.
DR GO; GO:0099078; C:BORC complex; ISO:MGI.
DR GO; GO:0098574; C:cytoplasmic side of lysosomal membrane; IC:ComplexPortal.
DR GO; GO:0031410; C:cytoplasmic vesicle; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0002177; C:manchette; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR GO; GO:0030141; C:secretory granule; ISS:UniProtKB.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000149; F:SNARE binding; ISO:MGI.
DR GO; GO:0008089; P:anterograde axonal transport; IMP:UniProtKB.
DR GO; GO:0048490; P:anterograde synaptic vesicle transport; IMP:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; IMP:MGI.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; TAS:ParkinsonsUK-UCL.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0008333; P:endosome to lysosome transport; ISO:MGI.
DR GO; GO:0051650; P:establishment of vesicle localization; IMP:MGI.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1902774; P:late endosome to lysosome transport; IMP:MGI.
DR GO; GO:0007042; P:lysosomal lumen acidification; IMP:MGI.
DR GO; GO:0032418; P:lysosome localization; ISS:UniProtKB.
DR GO; GO:0007040; P:lysosome organization; IMP:MGI.
DR GO; GO:0032438; P:melanosome organization; IC:ComplexPortal.
DR GO; GO:0010977; P:negative regulation of neuron projection development; IGI:ParkinsonsUK-UCL.
DR GO; GO:0070050; P:neuron cellular homeostasis; IMP:MGI.
DR GO; GO:0031175; P:neuron projection development; NAS:UniProtKB.
DR GO; GO:0072384; P:organelle transport along microtubule; IC:ComplexPortal.
DR GO; GO:0051604; P:protein maturation; IMP:MGI.
DR GO; GO:0031503; P:protein-containing complex localization; IMP:MGI.
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; ISO:MGI.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0008090; P:retrograde axonal transport; IMP:MGI.
DR GO; GO:0016079; P:synaptic vesicle exocytosis; ISO:MGI.
DR GO; GO:0031629; P:synaptic vesicle fusion to presynaptic active zone membrane; IMP:MGI.
DR GO; GO:0016188; P:synaptic vesicle maturation; IMP:MGI.
DR GO; GO:0048489; P:synaptic vesicle transport; ISS:UniProtKB.
DR GO; GO:0072553; P:terminal button organization; IMP:MGI.
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; Alternative splicing; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Exocytosis; Golgi apparatus; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Synapse.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT CHAIN 2..136
FT /note="SNARE-associated protein Snapin"
FT /id="PRO_0000097557"
FT REGION 83..136
FT /note="Interaction with TOR1A"
FT /evidence="ECO:0000250"
FT COILED 37..126
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 14
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 50
FT /note="Phosphoserine; by PKA; in vitro"
FT /evidence="ECO:0000269|PubMed:11283605"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O95295"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..54
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009165"
FT VAR_SEQ 55..63
FT /note="REQIDNLAT -> MLVAHFLFP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009166"
FT MUTAGEN 42
FT /note="S->A: No effect."
FT /evidence="ECO:0000269|PubMed:11283605"
FT MUTAGEN 50
FT /note="S->A: Inhibition of phosphorylation."
FT /evidence="ECO:0000269|PubMed:11283605"
FT MUTAGEN 50
FT /note="S->D: 3.5-fold increase in SNAP25 binding."
FT /evidence="ECO:0000269|PubMed:11283605"
FT MUTAGEN 63
FT /note="T->A: No effect."
FT /evidence="ECO:0000269|PubMed:11283605"
SQ SEQUENCE 136 AA; 14904 MW; C81AC2ABCDCA21FA CRC64;
MAAAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES QVELREQIDN
LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ NAQERLRRLN HSVAKETARR
RAMLDSGVYP PGSPSK
