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O95295

- SNAPN_HUMAN

UniProt

O95295 - SNAPN_HUMAN

Protein

SNARE-associated protein Snapin

Gene

SNAPIN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Component of the BLOC-1 complex, a complex that is required for normal biogenesis of lysosome-related organelles (LRO), such as platelet dense granules and melanosomes. In concert with the AP-3 complex, the BLOC-1 complex is required to target membrane protein cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals. The BLOC-1 complex, in association with SNARE proteins, is also proposed to be involved in neurite extension. Plays a role in intracellular vesicle trafficking and synaptic vesicle recycling. May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release through its ability to potentiate the interaction of synaptotagmin with the SNAREs and the plasma-membrane-associated protein SNAP25. Its phosphorylation state influences exocytotic protein interactions and may regulate synaptic vesicle exocytosis. May also have a role in the mechanisms of SNARE-mediated membrane fusion in non-neuronal cells.2 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. SNARE binding Source: MGI

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. anterograde synaptic vesicle transport Source: UniProtKB
    3. intracellular protein transport Source: ProtInc
    4. melanosome organization Source: UniProtKB
    5. neuron projection development Source: UniProtKB
    6. neurotransmitter secretion Source: ProtInc
    7. positive regulation of late endosome to lysosome transport Source: ParkinsonsUK-UCL
    8. regulation of protein binding Source: ParkinsonsUK-UCL
    9. synaptic vesicle exocytosis Source: MGI
    10. synaptic vesicle fusion to presynaptic membrane Source: Ensembl
    11. synaptic vesicle maturation Source: Ensembl
    12. synaptic vesicle transport Source: UniProtKB
    13. terminal button organization Source: Ensembl
    14. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Exocytosis, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_19400. Golgi Associated Vesicle Biogenesis.

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    SNARE-associated protein Snapin
    Alternative name(s):
    Biogenesis of lysosome-related organelles complex 1 subunit 7
    Short name:
    BLOC-1 subunit 7
    Synaptosomal-associated protein 25-binding protein
    Short name:
    SNAP-associated protein
    Gene namesi
    Name:SNAPIN
    Synonyms:BLOC1S7, SNAP25BP, SNAPAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:17145. SNAPIN.

    Subcellular locationi

    Cytoplasm By similarity. Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane Curated; Peripheral membrane protein Curated; Cytoplasmic side Curated. Cytoplasmperinuclear region 3 Publications. Golgi apparatus membrane By similarity. Cytoplasmic vesiclesecretory vesicle By similarity
    Note: May be cytoplasmic and peripheral membrane bound or anchored to the vesicular membrane through an N-terminal signal anchor By similarity. Colocalizes with NANOS1 and PUM2 in the perinuclear region of germ cells.By similarity

    GO - Cellular componenti

    1. BLOC-1 complex Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    4. Golgi apparatus Source: HPA
    5. Golgi membrane Source: UniProtKB-SubCell
    6. nucleolus Source: HPA
    7. perinuclear region of cytoplasm Source: UniProtKB
    8. secretory granule Source: UniProtKB
    9. synapse Source: MGI
    10. synaptic vesicle Source: UniProtKB
    11. synaptic vesicle membrane Source: UniProtKB-SubCell
    12. transport vesicle Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162404012.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 136135SNARE-associated protein SnapinPRO_0000097556Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei10 – 101Phosphoserine1 Publication
    Modified residuei14 – 141Phosphothreonine1 Publication
    Modified residuei50 – 501Phosphoserine; by PKABy similarity
    Modified residuei129 – 1291Phosphotyrosine1 Publication
    Modified residuei133 – 1331Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated by CSNK1D/CK1 By similarity. Phosphorylated by PKD, phosphorylation controls SNAPIN protein stability.By similarity5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95295.
    PaxDbiO95295.
    PeptideAtlasiO95295.
    PRIDEiO95295.

    PTM databases

    PhosphoSiteiO95295.

    Expressioni

    Tissue specificityi

    Expressed in male germ cells of adult testis (at protein level).1 Publication

    Developmental stagei

    Expressed in germ cells of 22-week prenatal testis.1 Publication

    Gene expression databases

    BgeeiO95295.
    CleanExiHS_SNAPIN.
    GenevestigatoriO95295.

    Organism-specific databases

    HPAiHPA046974.

    Interactioni

    Subunit structurei

    Interacts with CSNK1D, SNAP23 and STX4A but not with STX1A, VAMP2 and SYT1. Interacts with SNAP25; the interaction with SNAP25 is increased by its phosphorylation. Component of the biogenesis of lysosome-related organelles complex 1 (BLOC-1) composed of BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. Octamer composed of one copy each BLOC1S1, BLOC1S2, BLOC1S3, BLOC1S4, BLOC1S5, BLOC1S6, DTNBP1/BLOC1S7 and SNAPIN/BLOC1S8. The BLOC-1 complex associates with the AP-3 protein complex and membrane protein cargos. Associates with the SNARE complex. Interacts with CNTRL, NANOS1, PUM2 and RGS7. Interacts with TOR1A; the interaction is direct and associates SNAPIN with the CSN complex. Interacts with human cytomegalovirus/HHV-5 protein UL70.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BLOC1S2Q6QNY17EBI-296723,EBI-465872
    BLOC1S6Q9UL452EBI-296723,EBI-465781
    DTNBP1Q96EV84EBI-296723,EBI-465804
    DYSFO759233EBI-296723,EBI-2799016
    LRRK2Q5S0075EBI-296723,EBI-5323863
    SLC14A2Q15849-15EBI-296723,EBI-1633392
    Slc14a2Q62668-16EBI-296723,EBI-1635608From a different organism.
    SPTBP112773EBI-296723,EBI-514908

    Protein-protein interaction databases

    BioGridi117101. 32 interactions.
    IntActiO95295. 66 interactions.
    MINTiMINT-5002303.
    STRINGi9606.ENSP00000357674.

    Structurei

    3D structure databases

    ProteinModelPortaliO95295.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni83 – 13654Interaction with TOR1AAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili37 – 12690Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Belongs to the SNAPIN family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiNOG83669.
    HOGENOMiHOG000253926.
    HOVERGENiHBG056744.
    InParanoidiO95295.
    OMAiHVHSVRE.
    OrthoDBiEOG7SXW5D.
    PhylomeDBiO95295.
    TreeFamiTF319577.

    Family and domain databases

    InterProiIPR017246. Snapin.
    IPR028119. Snapin/Pallidin/Snn1.
    [Graphical view]
    PANTHERiPTHR31305. PTHR31305. 1 hit.
    PfamiPF14712. Snapin_Pallidin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037631. Snapin. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O95295-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAGAGSAAVS GAGTPVAGPT GRDLFAEGLL EFLRPAVQQL DSHVHAVRES    50
    QVELREQIDN LATELCRINE DQKVALDLDP YVKKLLNARR RVVLVNNILQ 100
    NAQERLRRLN HSVAKETARR RAMLDSGIYP PGSPGK 136
    Length:136
    Mass (Da):14,874
    Last modified:May 1, 1999 - v1
    Checksum:i3EA402AC53C81FFF
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti112 – 1121S → C.
    Corresponds to variant rs1802461 [ dbSNP | Ensembl ].
    VAR_017423

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086837 mRNA. Translation: AAD11417.1.
    AK024555 mRNA. Translation: BAB14927.1.
    BT006753 mRNA. Translation: AAP35399.1.
    AL592150 Genomic DNA. Translation: CAI18797.1.
    CH471121 Genomic DNA. Translation: EAW53288.1.
    CH471121 Genomic DNA. Translation: EAW53289.1.
    BC000761 mRNA. Translation: AAH00761.1.
    BC004494 mRNA. Translation: AAH04494.1.
    CCDSiCCDS1049.1.
    RefSeqiNP_036569.1. NM_012437.5.
    UniGeneiHs.32018.

    Genome annotation databases

    EnsembliENST00000368685; ENSP00000357674; ENSG00000143553.
    GeneIDi23557.
    KEGGihsa:23557.
    UCSCiuc001fcq.4. human.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF086837 mRNA. Translation: AAD11417.1 .
    AK024555 mRNA. Translation: BAB14927.1 .
    BT006753 mRNA. Translation: AAP35399.1 .
    AL592150 Genomic DNA. Translation: CAI18797.1 .
    CH471121 Genomic DNA. Translation: EAW53288.1 .
    CH471121 Genomic DNA. Translation: EAW53289.1 .
    BC000761 mRNA. Translation: AAH00761.1 .
    BC004494 mRNA. Translation: AAH04494.1 .
    CCDSi CCDS1049.1.
    RefSeqi NP_036569.1. NM_012437.5.
    UniGenei Hs.32018.

    3D structure databases

    ProteinModelPortali O95295.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117101. 32 interactions.
    IntActi O95295. 66 interactions.
    MINTi MINT-5002303.
    STRINGi 9606.ENSP00000357674.

    Protein family/group databases

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

    PTM databases

    PhosphoSitei O95295.

    Proteomic databases

    MaxQBi O95295.
    PaxDbi O95295.
    PeptideAtlasi O95295.
    PRIDEi O95295.

    Protocols and materials databases

    DNASUi 23557.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368685 ; ENSP00000357674 ; ENSG00000143553 .
    GeneIDi 23557.
    KEGGi hsa:23557.
    UCSCi uc001fcq.4. human.

    Organism-specific databases

    CTDi 23557.
    GeneCardsi GC01P153631.
    HGNCi HGNC:17145. SNAPIN.
    HPAi HPA046974.
    MIMi 607007. gene.
    neXtProti NX_O95295.
    PharmGKBi PA162404012.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG83669.
    HOGENOMi HOG000253926.
    HOVERGENi HBG056744.
    InParanoidi O95295.
    OMAi HVHSVRE.
    OrthoDBi EOG7SXW5D.
    PhylomeDBi O95295.
    TreeFami TF319577.

    Enzyme and pathway databases

    Reactomei REACT_19400. Golgi Associated Vesicle Biogenesis.

    Miscellaneous databases

    GeneWikii SNAPAP.
    GenomeRNAii 23557.
    NextBioi 46130.
    PROi O95295.
    SOURCEi Search...

    Gene expression databases

    Bgeei O95295.
    CleanExi HS_SNAPIN.
    Genevestigatori O95295.

    Family and domain databases

    InterProi IPR017246. Snapin.
    IPR028119. Snapin/Pallidin/Snn1.
    [Graphical view ]
    PANTHERi PTHR31305. PTHR31305. 1 hit.
    Pfami PF14712. Snapin_Pallidin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037631. Snapin. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "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: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Brain.
    2. "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].
      Tissue: Adipose tissue.
    3. "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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. 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].
      Tissue: Lung carcinoma and Melanoma.
    7. "Snapin interacts with the N-terminus of regulator of G protein signaling 7."
      Hunt R.A., Edris W., Chanda P.K., Nieuwenhuijsen B., Young K.H.
      Biochem. Biophys. Res. Commun. 303:594-599(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RGS7.
    8. "Identification of snapin and three novel proteins (BLOS1, BLOS2, and BLOS3/reduced pigmentation) as subunits of biogenesis of lysosome-related organelles complex-1 (BLOC-1)."
      Starcevic M., Dell'Angelica E.C.
      J. Biol. Chem. 279:28393-28401(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX.
    9. "Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission."
      Gromley A., Yeaman C., Rosa J., Redick S., Chen C.-T., Mirabelle S., Guha M., Sillibourne J., Doxsey S.J.
      Cell 123:75-87(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNTRL.
    10. "BLOC-1 is required for cargo-specific sorting from vacuolar early endosomes toward lysosome-related organelles."
      Setty S.R., Tenza D., Truschel S.T., Chou E., Sviderskaya E.V., Theos A.C., Lamoreux M.L., Di Pietro S.M., Starcevic M., Bennett D.C., Dell'Angelica E.C., Raposo G., Marks M.S.
      Mol. Biol. Cell 18:768-780(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "The dystonia-associated protein torsinA modulates synaptic vesicle recycling."
      Granata A., Watson R., Collinson L.M., Schiavo G., Warner T.T.
      J. Biol. Chem. 283:7568-7579(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN VESICLE RECYCLING, INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    14. "The SNARE-associated component SNAPIN binds PUMILIO2 and NANOS1 proteins in human male germ cells."
      Ginter-Matuszewska B., Spik A., Rembiszewska A., Koyias C., Kupryjanczyk J., Jaruzelska J.
      Mol. Hum. Reprod. 15:173-179(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PUM2 AND NANOS1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-129 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; THR-14 AND SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "CSN complex controls the stability of selected synaptic proteins via a torsinA-dependent process."
      Granata A., Koo S.J., Haucke V., Schiavo G., Warner T.T.
      EMBO J. 30:181-193(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TOR1A, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    19. "Human cytomegalovirus primase UL70 specifically interacts with cellular factor Snapin."
      Shen A., Lei J., Yang E., Pei Y., Chen Y.C., Gong H., Xiao G., Liu F.
      J. Virol. 85:11732-11741(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HHV-5 PROTEIN UL70.
    20. "Assembly and architecture of biogenesis of lysosome-related organelles complex-1 (BLOC-1)."
      Lee H.H., Nemecek D., Schindler C., Smith W.J., Ghirlando R., Steven A.C., Bonifacino J.S., Hurley J.H.
      J. Biol. Chem. 287:5882-5890(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN THE BLOC-1 COMPLEX, COMPOSITION OF THE BLOC-1 COMPLEX.
    21. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSNAPN_HUMAN
    AccessioniPrimary (citable) accession number: O95295
    Secondary accession number(s): D3DV56, Q5SXU8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 120 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3