Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P60880

- SNP25_HUMAN

UniProt

P60880 - SNP25_HUMAN

Protein

Synaptosomal-associated protein 25

Gene

SNAP25

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (13 Apr 2004)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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.

    Sites

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

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. energy reserve metabolic process Source: Reactome
    2. glutamate secretion Source: Reactome
    3. neurotransmitter secretion Source: Reactome
    4. neurotransmitter uptake Source: UniProtKB
    5. regulation of insulin secretion Source: UniProtKB
    6. small molecule metabolic process Source: Reactome
    7. synaptic transmission Source: UniProtKB
    8. synaptic vesicle docking involved in exocytosis Source: UniProtKB

    Enzyme and pathway databases

    ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_15293. Dopamine Neurotransmitter Release Cycle.
    REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
    REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
    REACT_15425. Serotonin Neurotransmitter Release Cycle.
    REACT_18325. Regulation of insulin secretion.
    REACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
    REACT_200658. Toxicity of botulinum toxin type C (BoNT/C).
    REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).
    REACT_23947. GABA synthesis, release, reuptake and degradation.

    Protein family/group databases

    TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:11132. SNAP25.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: UniProtKB
    3. growth cone Source: HGNC
    4. membrane Source: UniProtKB
    5. neuron projection Source: HGNC
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell
    7. plasma membrane Source: Reactome
    8. SNARE complex Source: UniProtKB
    9. synapse Source: UniProtKB-KW
    10. synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: Ensembl
    11. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

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

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA35980.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 206206Synaptosomal-associated protein 25PRO_0000213587Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi85 – 851S-palmitoyl cysteineBy similarity
    Lipidationi88 – 881S-palmitoyl cysteineBy similarity
    Lipidationi90 – 901S-palmitoyl cysteineBy similarity
    Lipidationi92 – 921S-palmitoyl cysteineBy similarity
    Modified residuei138 – 1381PhosphothreonineBy similarity
    Modified residuei187 – 1871PhosphoserineBy similarity

    Post-translational modificationi

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

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP60880.
    PaxDbiP60880.
    PRIDEiP60880.

    PTM databases

    PhosphoSiteiP60880.

    Miscellaneous databases

    PMAP-CutDBQ5U0B5.

    Expressioni

    Tissue specificityi

    Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum.

    Gene expression databases

    BgeeiP60880.
    CleanExiHS_SNAP25.
    GenevestigatoriP60880.

    Organism-specific databases

    HPAiCAB000360.
    HPA001830.

    Interactioni

    Subunit structurei

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

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ZDHHC17Q8IUH53EBI-524785,EBI-524753

    Protein-protein interaction databases

    BioGridi112500. 28 interactions.
    DIPiDIP-34554N.
    IntActiP60880. 11 interactions.
    MINTiMINT-1403389.

    Structurei

    Secondary structure

    1
    206
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi8 – 8073
    Helixi148 – 16720
    Beta strandi191 – 1933

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KILX-ray2.30C10-81[»]
    D139-204[»]
    1XTGX-ray2.10B146-204[»]
    3RK2X-ray2.20C/G7-82[»]
    D/H141-203[»]
    3RK3X-ray3.50C7-82[»]
    D141-203[»]
    3RL0X-ray3.80C/G/K/O/S/W/a/e7-82[»]
    D/H/L/P/T/X/b/f141-203[»]
    3ZURX-ray2.71A/B145-206[»]
    ProteinModelPortaliP60880.
    SMRiP60880. Positions 10-78, 141-204.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP60880.

    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 CENPFBy similarityAdd
    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.
    HOVERGENiHBG056971.
    KOiK18211.
    OMAiESADAYQ.
    OrthoDBiEOG75F4F5.
    PhylomeDBiP60880.
    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: P60880-1) [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: P60880-2) [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

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441I → V in BAD97337. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2. 5 PublicationsVSP_006186Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19760 mRNA. Translation: AAC37545.1.
    L19761 mRNA. Translation: AAC37546.1.
    D21267 mRNA. Translation: BAA22370.1.
    BT019684 mRNA. Translation: AAV38490.1.
    AK223617 mRNA. Translation: BAD97337.1.
    AK289647 mRNA. Translation: BAF82336.1.
    AK314359 mRNA. Translation: BAG36991.1.
    AL023913 Genomic DNA. Translation: CAB42860.1.
    AL023913 Genomic DNA. Translation: CAC34534.1.
    AL023913 Genomic DNA. Translation: CAD56158.1.
    CH471133 Genomic DNA. Translation: EAX10346.1.
    CH471133 Genomic DNA. Translation: EAX10349.1.
    CH471133 Genomic DNA. Translation: EAX10350.1.
    CH471133 Genomic DNA. Translation: EAX10352.1.
    BC010647 mRNA. Translation: AAH10647.1.
    CCDSiCCDS13109.1. [P60880-2]
    CCDS13110.1.
    PIRiI53735.
    I67823.
    RefSeqiNP_003072.2. NM_003081.3. [P60880-2]
    NP_570824.1. NM_130811.2. [P60880-1]
    XP_005260865.1. XM_005260808.2. [P60880-1]
    XP_005260867.1. XM_005260810.2. [P60880-2]
    UniGeneiHs.167317.

    Genome annotation databases

    EnsembliENST00000254976; ENSP00000254976; ENSG00000132639. [P60880-1]
    ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
    GeneIDi6616.
    KEGGihsa:6616.
    UCSCiuc002wnq.2. human.
    uc002wnr.2. human. [P60880-2]

    Polymorphism databases

    DMDMi46397726.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L19760 mRNA. Translation: AAC37545.1 .
    L19761 mRNA. Translation: AAC37546.1 .
    D21267 mRNA. Translation: BAA22370.1 .
    BT019684 mRNA. Translation: AAV38490.1 .
    AK223617 mRNA. Translation: BAD97337.1 .
    AK289647 mRNA. Translation: BAF82336.1 .
    AK314359 mRNA. Translation: BAG36991.1 .
    AL023913 Genomic DNA. Translation: CAB42860.1 .
    AL023913 Genomic DNA. Translation: CAC34534.1 .
    AL023913 Genomic DNA. Translation: CAD56158.1 .
    CH471133 Genomic DNA. Translation: EAX10346.1 .
    CH471133 Genomic DNA. Translation: EAX10349.1 .
    CH471133 Genomic DNA. Translation: EAX10350.1 .
    CH471133 Genomic DNA. Translation: EAX10352.1 .
    BC010647 mRNA. Translation: AAH10647.1 .
    CCDSi CCDS13109.1. [P60880-2 ]
    CCDS13110.1.
    PIRi I53735.
    I67823.
    RefSeqi NP_003072.2. NM_003081.3. [P60880-2 ]
    NP_570824.1. NM_130811.2. [P60880-1 ]
    XP_005260865.1. XM_005260808.2. [P60880-1 ]
    XP_005260867.1. XM_005260810.2. [P60880-2 ]
    UniGenei Hs.167317.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KIL X-ray 2.30 C 10-81 [» ]
    D 139-204 [» ]
    1XTG X-ray 2.10 B 146-204 [» ]
    3RK2 X-ray 2.20 C/G 7-82 [» ]
    D/H 141-203 [» ]
    3RK3 X-ray 3.50 C 7-82 [» ]
    D 141-203 [» ]
    3RL0 X-ray 3.80 C/G/K/O/S/W/a/e 7-82 [» ]
    D/H/L/P/T/X/b/f 141-203 [» ]
    3ZUR X-ray 2.71 A/B 145-206 [» ]
    ProteinModelPortali P60880.
    SMRi P60880. Positions 10-78, 141-204.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112500. 28 interactions.
    DIPi DIP-34554N.
    IntActi P60880. 11 interactions.
    MINTi MINT-1403389.

    Chemistry

    ChEMBLi CHEMBL2364159.
    DrugBanki DB00083. Botulinum Toxin Type A.

    Protein family/group databases

    TCDBi 1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

    PTM databases

    PhosphoSitei P60880.

    Polymorphism databases

    DMDMi 46397726.

    Proteomic databases

    MaxQBi P60880.
    PaxDbi P60880.
    PRIDEi P60880.

    Protocols and materials databases

    DNASUi 6616.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000254976 ; ENSP00000254976 ; ENSG00000132639 . [P60880-1 ]
    ENST00000304886 ; ENSP00000307341 ; ENSG00000132639 . [P60880-2 ]
    GeneIDi 6616.
    KEGGi hsa:6616.
    UCSCi uc002wnq.2. human.
    uc002wnr.2. human. [P60880-2 ]

    Organism-specific databases

    CTDi 6616.
    GeneCardsi GC20P010199.
    HGNCi HGNC:11132. SNAP25.
    HPAi CAB000360.
    HPA001830.
    MIMi 600322. gene.
    neXtProti NX_P60880.
    PharmGKBi PA35980.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG259235.
    HOVERGENi HBG056971.
    KOi K18211.
    OMAi ESADAYQ.
    OrthoDBi EOG75F4F5.
    PhylomeDBi P60880.
    TreeFami TF315125.

    Enzyme and pathway databases

    Reactomei REACT_12591. Glutamate Neurotransmitter Release Cycle.
    REACT_15293. Dopamine Neurotransmitter Release Cycle.
    REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
    REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
    REACT_15425. Serotonin Neurotransmitter Release Cycle.
    REACT_18325. Regulation of insulin secretion.
    REACT_200616. Toxicity of botulinum toxin type E (BoNT/E).
    REACT_200658. Toxicity of botulinum toxin type C (BoNT/C).
    REACT_200737. Toxicity of botulinum toxin type A (BoNT/A).
    REACT_23947. GABA synthesis, release, reuptake and degradation.

    Miscellaneous databases

    ChiTaRSi SNAP25. human.
    EvolutionaryTracei P60880.
    GeneWikii SNAP25.
    GenomeRNAii 6616.
    NextBioi 25761.
    PMAP-CutDB Q5U0B5.
    PROi P60880.
    SOURCEi Search...

    Gene expression databases

    Bgeei P60880.
    CleanExi HS_SNAP25.
    Genevestigatori P60880.

    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. "Human cDNA clones encoding two different isoforms of the nerve terminal protein SNAP-25."
      Bark I.C., Wilson M.C.
      Gene 139:291-292(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Fetal brain and Temporal cortex.
    2. "Cloning and sequence analysis of the human SNAP25 cDNA."
      Zhao N., Hashida H., Takahashi N., Sakaki Y.
      Gene 145:313-314(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Frontal cortex.
    3. "Insulin-responsive tissues contain the core complex protein SNAP-25 (synaptosomal-associated protein 25) A and B isoforms in addition to syntaxin 4 and synaptobrevins 1 and 2."
      Jagadish M.N., Fernandez C.S., Hewish D.R., Macaulay S.L., Gough K.H., Grusovin J., Verkuylen A., Cosgrove L., Alafaci A., Frenkel M.J., Ward C.W.
      Biochem. J. 317:945-954(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Skeletal muscle.
    4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Tissue: Amygdala and Hippocampus.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Brain.
    7. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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).
      Tissue: Eye.
    10. "SNAP-25 is also an iron-sulfur protein."
      Huang Q., Hong X., Hao Q.
      FEBS Lett. 582:1431-1436(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PUTATIVE IRON-SULFUR CLUSTER.
    11. "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)
      Cited for: ASSOCIATION WITH THE BLOC-1 COMPLEX, INTERACTION WITH BLOC1S6.
    12. "Three-dimensional structure of the complexin/SNARE complex."
      Chen X., Tomchick D.R., Kovrigin E., Arac D., Machius M., Suedhof T.C., Rizo J.
      Neuron 33:397-409(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 11-81 AND 141-202 IN COMPLEX WITH STX1A; CPLX1 AND VAMP2, STRUCTURE BY NMR.

    Entry informationi

    Entry nameiSNP25_HUMAN
    AccessioniPrimary (citable) accession number: P60880
    Secondary accession number(s): B2RAU4
    , D3DW16, D3DW17, P13795, P36974, P70557, P70558, Q53EM2, Q5U0B5, 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 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    When cloned and expressed in Eschericia coli, where protein palmitoylation does not occur, Cys-85, Cys-88, Cys-90 and Cys-92 in the protein sequence readily form an iron-sulfur cluster instead.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3