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P60879

- SNP25_MOUSE

UniProt

P60879 - SNP25_MOUSE

Protein

Synaptosomal-associated protein 25

Gene

Snap25

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei180 – 1812Cleavage; by BONT/EBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. SNARE binding Source: MGI
    3. syntaxin-1 binding Source: MGI

    GO - Biological processi

    1. long-term synaptic potentiation Source: MGI
    2. neurotransmitter secretion Source: MGI
    3. regulation of establishment of protein localization Source: MGI
    4. regulation of neuron projection development Source: ParkinsonsUK-UCL

    Enzyme and pathway databases

    ReactomeiREACT_205038. Acetylcholine Neurotransmitter Release Cycle.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Synaptosomal-associated protein 25
    Short name:
    SNAP-25
    Alternative name(s):
    Super protein
    Short name:
    SUP
    Synaptosomal-associated 25 kDa protein
    Gene namesi
    Name:Snap25
    Synonyms:Snap
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:98331. Snap25.

    Subcellular locationi

    Cytoplasmperinuclear region. Cell membrane; Lipid-anchor. Cell junctionsynapsesynaptosome
    Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region.

    GO - Cellular componenti

    1. axon Source: MGI
    2. axonal growth cone Source: MGI
    3. BLOC-1 complex Source: Ensembl
    4. cell junction Source: UniProtKB-KW
    5. cytoplasm Source: UniProtKB
    6. membrane Source: UniProtKB
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. plasma membrane Source: MGI
    9. SNARE complex Source: UniProtKB
    10. synapse Source: MGI
    11. synaptobrevin 2-SNAP-25-syntaxin-1a complex Source: MGI
    12. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: MGI
    13. trans-Golgi network Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi85 – 851C → S: 91% reduction in palmitoylation level. 14% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-88 or A-88. 1 Publication
    Mutagenesisi88 – 881C → S: 79% reduction in palmitoylation level. 18% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-85 or A-85. 1 Publication
    Mutagenesisi90 – 901C → S: 58% reduction in palmitoylation level. 28% membrane association. Very little palmitoylation and less than 8% membrane association; when associated with S-92 or A-92. 1 Publication
    Mutagenesisi92 – 921C → S: 65% reduction in palmitoylation level. 29% membrane association. No palmitoylation and less than 8% membrane association; when associated with S-90 or A-90. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206Synaptosomal-associated protein 25PRO_0000213589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi85 – 851S-palmitoyl cysteine1 Publication
    Lipidationi88 – 881S-palmitoyl cysteine1 Publication
    Lipidationi90 – 901S-palmitoyl cysteine1 Publication
    Lipidationi92 – 921S-palmitoyl cysteine1 Publication
    Modified residuei138 – 1381Phosphothreonine; by PKC and PKA1 Publication
    Modified residuei187 – 1871Phosphoserine; by PKC1 Publication

    Post-translational modificationi

    Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association.1 Publication

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP60879.
    PaxDbiP60879.
    PRIDEiP60879.

    PTM databases

    PhosphoSiteiP60879.

    Expressioni

    Gene expression databases

    BgeeiP60879.
    CleanExiMM_SNAP25.
    GenevestigatoriP60879.

    Interactioni

    Subunit structurei

    Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with TRIM9, RIMS1, SNAPIN and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8 By similarity. Found in a complex containing SYT1, SV2B and syntaxin-1. Interacts with CENPF and OTOF. Associates with the BLOC-1 complex. Isoform 1 and isoform 2 interact with BLOC1S6. Interacts with EQTN.By similarity6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CenpfQ155P713EBI-445270,EBI-2211248
    Vamp2P630445EBI-445270,EBI-521920

    Protein-protein interaction databases

    BioGridi203362. 15 interactions.
    DIPiDIP-29066N.
    IntActiP60879. 37 interactions.
    MINTiMINT-2411221.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi21 – 7353
    Turni74 – 763
    Helixi77 – 815
    Turni140 – 1434
    Helixi144 – 20259
    Turni203 – 2053

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BU0model-C18-82[»]
    D139-206[»]
    ProteinModelPortaliP60879.
    SMRiP60879. Positions 10-78, 141-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini19 – 8163t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini140 – 20263t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 7575Interaction with CENPFAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi85 – 928Cys-rich

    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.
    HOVERGENiHBG056971.
    InParanoidiA2AIC2.
    KOiK18211.
    OMAiESADAYQ.
    OrthoDBiEOG75F4F5.
    PhylomeDBiP60879.
    TreeFamiTF315125.

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Note: Isoforms differ by the usage of two alternative homologous exons (5a and 5b) which code for positions 56 to 94 and differ only in 9 positions out of 39.

    Isoform 1 (identifier: P60879-1) [UniParc]FASTAAdd to Basket

    Also known as: SNAP-25b

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML    50
    DEQGEQLERI EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA 100
    YKKAWGNNQD GVVASQPARV VDEREQMAIS GGFIRRVTND ARENEMDENL 150
    EQVSGIIGNL RHMALDMGNE IDTQNRQIDR IMEKADSNKT RIDEANQRAT 200
    KMLGSG 206
    Length:206
    Mass (Da):23,315
    Last modified:April 13, 2004 - v1
    Checksum:iFBED2B082A4CB6A6
    GO
    Isoform 2 (identifier: P60879-2) [UniParc] [UniParc]FASTAAdd to Basket

    Also known as: SNAP-25a

    The sequence of this isoform differs from the canonical sequence as follows:
         58-89: ERIEEGMDQINKDMKEAEKNLTDLGKFCGLCV → DRVEEGMNHINQDMKEAEKNLKDLGKCCGLFI

    Show »
    Length:206
    Mass (Da):23,336
    Checksum:iE272652C701EA984
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2. 3 PublicationsVSP_010019Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22012 mRNA. Translation: AAA61741.1.
    AF483516 mRNA. Translation: AAL90790.1.
    AF483517 mRNA. Translation: AAL90791.1.
    AK078038 mRNA. Translation: BAC37105.1.
    AL732447 Genomic DNA. Translation: CAM15064.1.
    AL732447 Genomic DNA. Translation: CAM15065.1.
    CH466519 Genomic DNA. Translation: EDL28390.1.
    BC018249 mRNA. Translation: AAH18249.1.
    CCDSiCCDS16793.1.
    CCDS71153.1. [P60879-2]
    PIRiA33623.
    RefSeqiNP_001277985.1. NM_001291056.1. [P60879-2]
    NP_035558.1. NM_011428.3. [P60879-1]
    UniGeneiMm.45953.

    Genome annotation databases

    EnsembliENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273. [P60879-1]
    ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273. [P60879-2]
    GeneIDi20614.
    KEGGimmu:20614.
    UCSCiuc008mop.1. mouse.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M22012 mRNA. Translation: AAA61741.1 .
    AF483516 mRNA. Translation: AAL90790.1 .
    AF483517 mRNA. Translation: AAL90791.1 .
    AK078038 mRNA. Translation: BAC37105.1 .
    AL732447 Genomic DNA. Translation: CAM15064.1 .
    AL732447 Genomic DNA. Translation: CAM15065.1 .
    CH466519 Genomic DNA. Translation: EDL28390.1 .
    BC018249 mRNA. Translation: AAH18249.1 .
    CCDSi CCDS16793.1.
    CCDS71153.1. [P60879-2 ]
    PIRi A33623.
    RefSeqi NP_001277985.1. NM_001291056.1. [P60879-2 ]
    NP_035558.1. NM_011428.3. [P60879-1 ]
    UniGenei Mm.45953.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BU0 model - C 18-82 [» ]
    D 139-206 [» ]
    ProteinModelPortali P60879.
    SMRi P60879. Positions 10-78, 141-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 203362. 15 interactions.
    DIPi DIP-29066N.
    IntActi P60879. 37 interactions.
    MINTi MINT-2411221.

    PTM databases

    PhosphoSitei P60879.

    Proteomic databases

    MaxQBi P60879.
    PaxDbi P60879.
    PRIDEi P60879.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028727 ; ENSMUSP00000028727 ; ENSMUSG00000027273 . [P60879-1 ]
    ENSMUST00000110098 ; ENSMUSP00000105725 ; ENSMUSG00000027273 . [P60879-2 ]
    GeneIDi 20614.
    KEGGi mmu:20614.
    UCSCi uc008mop.1. mouse.

    Organism-specific databases

    CTDi 6616.
    MGIi MGI:98331. Snap25.

    Phylogenomic databases

    eggNOGi NOG259235.
    GeneTreei ENSGT00390000012186.
    HOVERGENi HBG056971.
    InParanoidi A2AIC2.
    KOi K18211.
    OMAi ESADAYQ.
    OrthoDBi EOG75F4F5.
    PhylomeDBi P60879.
    TreeFami TF315125.

    Enzyme and pathway databases

    Reactomei REACT_205038. Acetylcholine Neurotransmitter Release Cycle.

    Miscellaneous databases

    ChiTaRSi SNAP25. mouse.
    NextBioi 298983.
    PROi P60879.
    SOURCEi Search...

    Gene expression databases

    Bgeei P60879.
    CleanExi MM_SNAP25.
    Genevestigatori P60879.

    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. "The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations."
      Oyler G.A., Higgins G.A., Hart R.A., Battenberg E., Billingsley M., Bloom F.E., Wilson M.C.
      J. Cell Biol. 109:3039-3052(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION.
      Strain: BALB/c.
    2. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
      Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
      Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: ILS and ISS.
    3. "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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Eye.
    7. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 18-31; 60-72; 125-135 AND 143-176, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    8. "Characterization of the palmitoylation domain of SNAP-25."
      Lane S.R., Liu Y.
      J. Neurochem. 69:1864-1869(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PALMITOYLATION AT CYS-85; CYS-88; CYS-90 AND CYS-92, MUTAGENESIS OF CYS-85; CYS-88; CYS-90 AND CYS-92.
    9. "Snapin: a SNARE-associated protein implicated in synaptic transmission."
      Ilardi J.M., Mochida S., Sheng Z.-H.
      Nat. Neurosci. 2:119-124(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SNAPIN.
    10. "Differential phosphorylation of SNAP-25 in vivo by protein kinase C and protein kinase A."
      Hepp R., Cabaniols J.-P., Roche P.A.
      FEBS Lett. 532:52-56(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-138 AND SER-187.
    11. Cited for: INTERACTION WITH SYT1; SV2B AND SYNTAXIN-1.
    12. "Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse."
      Roux I., Safieddine S., Nouvian R., Grati M., Simmler M.-C., Bahloul A., Perfettini I., Le Gall M., Rostaing P., Hamard G., Triller A., Avan P., Moser T., Petit C.
      Cell 127:277-289(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH OTOF.
      Strain: BALB/c.
      Tissue: Cochlea.
    13. "CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25."
      Pooley R.D., Reddy S., Soukoulis V., Roland J.T., Goldenring J.R., Bader D.M.
      Mol. Biol. Cell 17:3176-3186(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CENPF.
    14. "Acrosome formation-associated factor is involved in fertilization."
      Hu X.Q., Ji S.Y., Li Y.C., Fan C.H., Cai H., Yang J.L., Zhang C.P., Chen M., Pan Z.F., Hu Z.Y., Gao F., Liu Y.X.
      Fertil. Steril. 93:1482-1492(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EQTN.
    15. "The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth."
      Ghiani C.A., Starcevic M., Rodriguez-Fernandez I.A., Nazarian R., Cheli V.T., Chan L.N., Malvar J.S., de Vellis J., Sabatti C., Dell'Angelica E.C.
      Mol. Psychiatry 15:204-215(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ASSOCIATION WITH THE BLOC-1 COMPLEX, SUBCELLULAR LOCATION, INTERACTION WITH BLOC1S6.
    16. "The synaptic SNARE complex is a parallel four-stranded helical bundle."
      Poirier M.A., Xiao W., Macosko J.C., Chan C., Shin Y.K., Bennett M.K.
      Nat. Struct. Biol. 5:765-769(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: 3D-STRUCTURE MODELING OF 18-206 IN COMPLEX WITH VAMP2 AND STX1A.

    Entry informationi

    Entry nameiSNP25_MOUSE
    AccessioniPrimary (citable) accession number: P60879
    Secondary accession number(s): A2AIC2
    , A2AIC3, P13795, P36974, P70557, P70558, Q8IXK3, Q96FM2, Q9BR45
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 116 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3