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O09044

- SNP23_MOUSE

UniProt

O09044 - SNP23_MOUSE

Protein

Synaptosomal-associated protein 23

Gene

Snap23

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    Functioni

    Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.By similarity

    GO - Molecular functioni

    1. protein binding Source: MGI

    GO - Biological processi

    1. exocytosis Source: MGI
    2. protein transport Source: UniProtKB-KW

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synaptosomal-associated protein 23
    Short name:
    SNAP-23
    Alternative name(s):
    Syndet
    Vesicle-membrane fusion protein SNAP-23
    Gene namesi
    Name:Snap23
    Synonyms:Sndt
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:109356. Snap23.

    Subcellular locationi

    Cell membrane; Peripheral membrane protein. Cell membrane By similarity; Lipid-anchor By similarity. Cell junctionsynapsesynaptosome
    Note: Mainly localized to the plasma membrane.

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasmic vesicle Source: MGI
    3. neuron projection Source: UniProtKB-SubCell
    4. plasma membrane Source: MGI
    5. synapse Source: UniProtKB-KW

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 210210Synaptosomal-associated protein 23PRO_0000213599Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei20 – 201Phosphoserine1 Publication
    Modified residuei23 – 231Phosphoserine1 Publication
    Modified residuei34 – 341Phosphoserine1 Publication
    Lipidationi79 – 791S-palmitoyl cysteineBy similarity
    Lipidationi80 – 801S-palmitoyl cysteineBy similarity
    Lipidationi83 – 831S-palmitoyl cysteineBy similarity
    Lipidationi85 – 851S-palmitoyl cysteineBy similarity
    Lipidationi87 – 871S-palmitoyl cysteineBy similarity
    Modified residuei110 – 1101Phosphoserine2 Publications

    Keywords - PTMi

    Acetylation, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiO09044.
    PaxDbiO09044.
    PRIDEiO09044.

    PTM databases

    PhosphoSiteiO09044.

    Expressioni

    Tissue specificityi

    Expressed in non-neuronal tissues.

    Gene expression databases

    ArrayExpressiO09044.
    BgeeiO09044.
    CleanExiMM_SNAP23.
    GenevestigatoriO09044.

    Interactioni

    Subunit structurei

    Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3. Binds simultaneously to SNAPIN and SYN4. Found in a complex with VAMP8 and STX1A By similarity. Binds tightly to multiple syntaxins and synaptobrevins/VAMPs. Found in a complex with VAMP8 and STX4 in pancreas. Interacts with STX1A and STX12.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi203367. 7 interactions.
    DIPiDIP-41401N.
    IntActiO09044. 6 interactions.
    MINTiMINT-269238.

    Structurei

    3D structure databases

    ProteinModelPortaliO09044.
    SMRiO09044. Positions 23-76, 146-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini14 – 7663t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini145 – 20763t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili23 – 7654By similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNAP-25 family.Curated
    Contains 2 t-SNARE coiled-coil homology domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG259235.
    GeneTreeiENSGT00390000012186.
    HOGENOMiHOG000231599.
    HOVERGENiHBG056971.
    KOiK08508.
    OrthoDBiEOG75F4F5.
    PhylomeDBiO09044.

    Family and domain databases

    InterProiIPR000928. SNAP-25.
    IPR000727. T_SNARE_dom.
    [Graphical view]
    PfamiPF00835. SNAP-25. 1 hit.
    PF05739. SNARE. 1 hit.
    [Graphical view]
    SMARTiSM00397. t_SNARE. 2 hits.
    [Graphical view]
    PROSITEiPS50192. T_SNARE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    O09044-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDNLSPEEVQ LRAHQVTDES LESTRRILGL AIESQDAGIK TITMLDEQGE    50
    QLNRIEEGMD QINKDMREAE KTLTELNKCC GLCICPCNRT KNFESGKNYK 100
    ATWGDGGDNS PSNVVSKQPS RITNGQPQQT TGAASGGYIK RITNDAREDE 150
    MEENLTQVGS ILGNLKNMAL DMGNEIDAQN QQIQKITEKA DTNKNRIDIA 200
    NTRAKKLIDS 210
    Length:210
    Mass (Da):23,261
    Last modified:July 1, 1997 - v1
    Checksum:i6919E127E16BA2C9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti6 – 61P → S in AAB62932. 1 PublicationCurated
    Sequence conflicti204 – 2041A → P in AAB62932. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000822 mRNA. Translation: BAA20345.1.
    U73143 mRNA. Translation: AAB53597.1.
    AF007169 mRNA. Translation: AAB62932.1.
    AF213257
    , AF213251, AF213252, AF213253, AF213254, AF213255, AF213256 Genomic DNA. Translation: AAF23503.1.
    AK019162 mRNA. Translation: BAB31577.1.
    BC070456 mRNA. Translation: AAH70456.1.
    CCDSiCCDS16622.1.
    PIRiJC5512.
    RefSeqiNP_001171263.1. NM_001177792.1.
    NP_001171264.1. NM_001177793.1.
    NP_033248.1. NM_009222.3.
    XP_006499120.1. XM_006499057.1.
    UniGeneiMm.245715.

    Genome annotation databases

    EnsembliENSMUST00000028743; ENSMUSP00000028743; ENSMUSG00000027287.
    ENSMUST00000110711; ENSMUSP00000106339; ENSMUSG00000027287.
    GeneIDi20619.
    KEGGimmu:20619.
    UCSCiuc008lwg.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB000822 mRNA. Translation: BAA20345.1 .
    U73143 mRNA. Translation: AAB53597.1 .
    AF007169 mRNA. Translation: AAB62932.1 .
    AF213257
    , AF213251 , AF213252 , AF213253 , AF213254 , AF213255 , AF213256 Genomic DNA. Translation: AAF23503.1 .
    AK019162 mRNA. Translation: BAB31577.1 .
    BC070456 mRNA. Translation: AAH70456.1 .
    CCDSi CCDS16622.1.
    PIRi JC5512.
    RefSeqi NP_001171263.1. NM_001177792.1.
    NP_001171264.1. NM_001177793.1.
    NP_033248.1. NM_009222.3.
    XP_006499120.1. XM_006499057.1.
    UniGenei Mm.245715.

    3D structure databases

    ProteinModelPortali O09044.
    SMRi O09044. Positions 23-76, 146-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203367. 7 interactions.
    DIPi DIP-41401N.
    IntActi O09044. 6 interactions.
    MINTi MINT-269238.

    PTM databases

    PhosphoSitei O09044.

    Proteomic databases

    MaxQBi O09044.
    PaxDbi O09044.
    PRIDEi O09044.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028743 ; ENSMUSP00000028743 ; ENSMUSG00000027287 .
    ENSMUST00000110711 ; ENSMUSP00000106339 ; ENSMUSG00000027287 .
    GeneIDi 20619.
    KEGGi mmu:20619.
    UCSCi uc008lwg.1. mouse.

    Organism-specific databases

    CTDi 8773.
    MGIi MGI:109356. Snap23.

    Phylogenomic databases

    eggNOGi NOG259235.
    GeneTreei ENSGT00390000012186.
    HOGENOMi HOG000231599.
    HOVERGENi HBG056971.
    KOi K08508.
    OrthoDBi EOG75F4F5.
    PhylomeDBi O09044.

    Enzyme and pathway databases

    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.

    Miscellaneous databases

    NextBioi 299005.
    PROi O09044.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O09044.
    Bgeei O09044.
    CleanExi MM_SNAP23.
    Genevestigatori O09044.

    Family and domain databases

    InterProi IPR000928. SNAP-25.
    IPR000727. T_SNARE_dom.
    [Graphical view ]
    Pfami PF00835. SNAP-25. 1 hit.
    PF05739. SNARE. 1 hit.
    [Graphical view ]
    SMARTi SM00397. t_SNARE. 2 hits.
    [Graphical view ]
    PROSITEi PS50192. T_SNARE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Adipose tissue.
    2. "Syndet is a novel SNAP-25 related protein expressed in many tissues."
      Wang G., Witkin J.W., Hao G., Bankaitis V.A., Scherer P.E., Baldini G.
      J. Cell Sci. 110:505-513(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "SNARE expression in mouse plasma cells."
      Olken S.K., Doerre S., Corley R.B.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "Structure and chromosomal localization of the mouse SNAP-23 gene."
      Vaidyanathan V.V., Roche P.A.
      Gene 247:181-189(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/SvJ.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Embryo.
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6.
      Tissue: Eye.
    7. "Syntaxin 12, a member of the syntaxin family localized to the endosome."
      Tang B.L., Tan A.E., Lim L.K., Lee S.S., Low D.Y., Hong W.
      J. Biol. Chem. 273:6944-6950(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH STX1A AND STX12.
    8. "A role of VAMP8/endobrevin in regulated exocytosis of pancreatic acinar cells."
      Wang C.-C., Ng C.P., Lu L., Atlashkin V., Zhang W., Seet L.-F., Hong W.
      Dev. Cell 7:359-371(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX4.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    10. "Specific phosphopeptide enrichment with immobilized titanium ion affinity chromatography adsorbent for phosphoproteome analysis."
      Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.
      J. Proteome Res. 7:3957-3967(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    11. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-34 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNP23_MOUSE
    AccessioniPrimary (citable) accession number: O09044
    Secondary accession number(s): O35620
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 115 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3