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Showing Protein SNARE-associated protein Snapin (HMDBP07999)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 1 metabolite
Identification
HMDB Protein ID HMDBP07999
Secondary Accession Numbers
  • 13710
Name SNARE-associated protein Snapin
Synonyms
  1. SNAP-associated protein
  2. Synaptosomal-associated protein 25-binding protein
Gene Name SNAPIN
Protein Type Unknown
Biological Properties
General Function Involved in SNARE binding
Specific Function May modulate a step between vesicle priming, fusion and calcium-dependent neurotransmitter release by potentiating the interaction of synaptotagmins 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
Pathways Not Available
Reactions Not Available
GO Classification Not Available
Cellular Location
  1. Cytoplasm
  2. Peripheral membrane protein
  3. Peripheral membrane protein
  4. Peripheral membrane protein
  5. Cytoplasmic vesicle
  6. Membrane
  7. Cytoplasmic side
  8. Cytoplasmic side
  9. secretory vesicle
  10. Cytoplasmic side (Potential)
  11. Cell junction
  12. synapse
  13. Cytoplasmic vesicle membrane
  14. synaptosome
  15. synaptic vesicle membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 1q21.3
SNPs SNAPIN
Gene Sequence 
>411 bp
ATGGCGGGGGCTGGTTCCGCCGCTGTATCGGGGGCAGGGACCCCGGTGGCGGGGCCCACA
GGCCGCGACCTTTTCGCCGAAGGGCTGCTGGAGTTCCTGCGACCCGCTGTGCAGCAGCTC
GACTCTCACGTACACGCCGTCAGAGAGAGCCAGGTAGAGCTCCGGGAACAAATTGACAAC
CTAGCCACAGAACTGTGCCGCATAAATGAGGATCAGAAGGTGGCCCTGGATCTTGACCCC
TATGTTAAGAAGCTACTTAATGCCCGGCGACGCGTTGTCTTGGTTAACAACATTCTACAG
AATGCTCAGGAACGACTGAGACGGCTAAACCACAGTGTTGCCAAGGAAACAGCCCGCAGG
AGAGCAATGCTGGATTCGGGAATTTACCCCCCTGGCTCCCCAGGCAAATAA
Protein Properties
Number of Residues 136
Molecular Weight 14873.8
Theoretical pI 9.78
Pfam Domain Function Not Available
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>SNARE-associated protein Snapin
MAGAGSAAVSGAGTPVAGPTGRDLFAEGLLEFLRPAVQQLDSHVHAVRESQVELREQIDN
LATELCRINEDQKVALDLDPYVKKLLNARRRVVLVNNILQNAQERLRRLNHSVAKETARR
RAMLDSGIYPPGSPGK
GenBank ID Protein 4206088
UniProtKB/Swiss-Prot ID O95295
UniProtKB/Swiss-Prot Entry Name SNAPN_HUMAN
PDB IDs Not Available
GenBank Gene ID AF086837
GeneCard ID SNAPIN
GenAtlas ID SNAPIN
HGNC ID HGNC:17145
References
General References
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  4. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
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  6. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  7. Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed:17287340 ]
  8. Ilardi JM, Mochida S, Sheng ZH: Snapin: a SNARE-associated protein implicated in synaptic transmission. Nat Neurosci. 1999 Feb;2(2):119-24. [PubMed:10195194 ]
  9. Hunt RA, Edris W, Chanda PK, Nieuwenhuijsen B, Young KH: Snapin interacts with the N-terminus of regulator of G protein signaling 7. Biochem Biophys Res Commun. 2003 Apr 4;303(2):594-9. [PubMed:12659861 ]
  10. Starcevic M, Dell'Angelica EC: 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). J Biol Chem. 2004 Jul 2;279(27):28393-401. Epub 2004 Apr 21. [PubMed:15102850 ]
  11. Gromley A, Yeaman C, Rosa J, Redick S, Chen CT, Mirabelle S, Guha M, Sillibourne J, Doxsey SJ: Centriolin anchoring of exocyst and SNARE complexes at the midbody is required for secretory-vesicle-mediated abscission. Cell. 2005 Oct 7;123(1):75-87. [PubMed:16213214 ]