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P60879 (SNP25_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptosomal-associated protein 25

Short name=SNAP-25
Alternative name(s):
Super protein
Short name=SUP
Synaptosomal-associated 25 kDa protein
Gene names
Name:Snap25
Synonyms:Snap
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length206 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.13

Subunit structure

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. Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15

Subcellular location

Cytoplasmperinuclear region. Cell membrane; Lipid-anchor. Cell junctionsynapsesynaptosome. Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Ref.1 Ref.13 Ref.15

Post-translational modification

Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association. Ref.8

Sequence similarities

Belongs to the SNAP-25 family.

Contains 2 t-SNARE coiled-coil homology domains.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cytoplasm
Membrane
Synapse
Synaptosome
   Coding sequence diversityAlternative splicing
   DomainCoiled coil
Repeat
   PTMLipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processneurotransmitter secretion

Inferred from mutant phenotype PubMed 11753414. Source: MGI

   Cellular_componentBLOC-1 complex

Inferred from electronic annotation. Source: Ensembl

SNARE complex

Inferred from sequence or structural similarity. Source: UniProtKB

axon

Inferred from sequence orthology PubMed 10712642. Source: MGI

axonal growth cone

Inferred from sequence orthology PubMed 10712642. Source: MGI

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay Ref.15. Source: UniProtKB

membrane

Inferred from direct assay Ref.15. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 18827011. Source: UniProtKB

plasma membrane

Traceable author statement PubMed 12145198. Source: MGI

synapse

Inferred from direct assay PubMed 10712642. Source: MGI

synaptobrevin 2-SNAP-25-syntaxin-1a complex

Inferred from sequence orthology PubMed 7553862. Source: MGI

synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex

Inferred from direct assay PubMed 21040848. Source: MGI

trans-Golgi network

Inferred from direct assay PubMed 18827011. Source: UniProtKB

   Molecular_functionSNARE binding

Inferred from direct assay PubMed 12145198. Source: MGI

syntaxin-1 binding

Inferred from sequence orthology PubMed 7553862. Source: MGI

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CenpfQ155P713EBI-445270,EBI-2211248
Vamp2P630445EBI-445270,EBI-521920

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform 2 (identifier: P60879-2)

Also known as: SNAP-25a;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 206206Synaptosomal-associated protein 25
PRO_0000213589

Regions

Domain19 – 8163t-SNARE coiled-coil homology 1
Domain140 – 20263t-SNARE coiled-coil homology 2
Region1 – 7575Interaction with CENPF
Compositional bias85 – 928Cys-rich

Sites

Site180 – 1812Cleavage; by BONT/E By similarity

Amino acid modifications

Modified residue1381Phosphothreonine; by PKC and PKA Ref.10
Modified residue1871Phosphoserine; by PKC Ref.10
Lipidation851S-palmitoyl cysteine Ref.8
Lipidation881S-palmitoyl cysteine Ref.8
Lipidation901S-palmitoyl cysteine Ref.8
Lipidation921S-palmitoyl cysteine Ref.8

Natural variations

Alternative sequence58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2.
VSP_010019

Experimental info

Mutagenesis851C → 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. Ref.8
Mutagenesis881C → 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. Ref.8
Mutagenesis901C → 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. Ref.8
Mutagenesis921C → 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. Ref.8

Secondary structure

......... 206
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (SNAP-25b) [UniParc].

Last modified April 13, 2004. Version 1.
Checksum: FBED2B082A4CB6A6

FASTA20623,315
        10         20         30         40         50         60 
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLERI 

        70         80         90        100        110        120 
EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA YKKAWGNNQD GVVASQPARV 

       130        140        150        160        170        180 
VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR 

       190        200 
IMEKADSNKT RIDEANQRAT KMLGSG 

« Hide

Isoform 2 (SNAP-25a) [UniParc] [UniParc].

Checksum: E272652C701EA984
Show »

FASTA20623,336

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"SV2B regulates synaptotagmin 1 by direct interaction."
Lazzell D.R., Belizaire R., Thakur P., Sherry D.M., Janz R.
J. Biol. Chem. 279:52124-52131(2004) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA33623.
RefSeqNP_035558.1. NM_011428.3.
XP_006499115.1. XM_006499052.1.
UniGeneMm.45953.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BU0model-C18-82[»]
D139-206[»]
ProteinModelPortalP60879.
SMRP60879. Positions 10-78, 141-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid203362. 15 interactions.
DIPDIP-29066N.
DIP-65N.
IntActP60879. 36 interactions.
MINTMINT-2411221.

PTM databases

PhosphoSiteP60879.

Proteomic databases

PaxDbP60879.
PRIDEP60879.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028727; ENSMUSP00000028727; ENSMUSG00000027273. [P60879-1]
ENSMUST00000110098; ENSMUSP00000105725; ENSMUSG00000027273. [P60879-2]
GeneID20614.
KEGGmmu:20614.
UCSCuc008mop.1. mouse.

Organism-specific databases

CTD6616.
MGIMGI:98331. Snap25.

Phylogenomic databases

eggNOGNOG259235.
GeneTreeENSGT00390000012186.
HOVERGENHBG056971.
InParanoidA2AIC2.
KOK08508.
OMAESADAYQ.
OrthoDBEOG75F4F5.
PhylomeDBP60879.
TreeFamTF315125.

Enzyme and pathway databases

ReactomeREACT_188937. Metabolism.

Gene expression databases

BgeeP60879.
CleanExMM_SNAP25.
GenevestigatorP60879.

Family and domain databases

InterProIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEPS50192. T_SNARE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSNAP25. mouse.
NextBio298983.
PROP60879.
SOURCESearch...

Entry information

Entry nameSNP25_MOUSE
AccessionPrimary (citable) accession number: P60879
Secondary accession number(s): A2AIC2 expand/collapse secondary AC list , A2AIC3, P13795, P36974, P70557, P70558, Q8IXK3, Q96FM2, Q9BR45
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot