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P60880 (SNP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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.

Subunit structure

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. Ref.11

Subcellular location

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.

Tissue specificity

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

Post-translational modification

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

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.

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
Reference proteome
Gene Ontology (GO)
   Biological_processenergy reserve metabolic process

Traceable author statement. Source: Reactome

glutamate secretion

Traceable author statement. Source: Reactome

neurotransmitter secretion

Traceable author statement. Source: Reactome

neurotransmitter uptake

Non-traceable author statement Ref.3. Source: UniProtKB

regulation of insulin secretion

Traceable author statement PubMed 15537656. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic transmission

Non-traceable author statement Ref.3. Source: UniProtKB

synaptic vesicle docking involved in exocytosis

Non-traceable author statement Ref.3. Source: UniProtKB

   Cellular_componentSNARE complex

Inferred from direct assay PubMed 19546860. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

growth cone

Inferred from sequence or structural similarity. Source: HGNC

membrane

Inferred from sequence or structural similarity. Source: UniProtKB

neuron projection

Inferred from sequence or structural similarity. Source: HGNC

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: UniProtKB-KW

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

Inferred from electronic annotation. Source: Ensembl

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

ZDHHC17Q8IUH53EBI-524785,EBI-524753

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: P60880-1)

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: P60880-2)

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_0000213587

Regions

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

Sites

Site180 – 1812Cleavage; by BONT/E

Amino acid modifications

Modified residue1381Phosphothreonine By similarity
Modified residue1871Phosphoserine By similarity
Lipidation851S-palmitoyl cysteine By similarity
Lipidation881S-palmitoyl cysteine By similarity
Lipidation901S-palmitoyl cysteine By similarity
Lipidation921S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2.
VSP_006186

Experimental info

Sequence conflict441I → V in BAD97337. Ref.5

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]"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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRI53735.
I67823.
RefSeqNP_003072.2. NM_003081.3.
NP_570824.1. NM_130811.2.
XP_005260865.1. XM_005260808.2.
XP_005260867.1. XM_005260810.2.
UniGeneHs.167317.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30C11-81[»]
D141-203[»]
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[»]
ProteinModelPortalP60880.
SMRP60880. Positions 10-78, 141-204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112500. 28 interactions.
DIPDIP-34554N.
IntActP60880. 11 interactions.
MINTMINT-1403389.

Chemistry

ChEMBLCHEMBL2364159.
DrugBankDB00083. Botulinum Toxin Type A.

Protein family/group databases

TCDB1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteP60880.

Polymorphism databases

DMDM46397726.

Proteomic databases

PaxDbP60880.
PRIDEP60880.

Protocols and materials databases

DNASU6616.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254976; ENSP00000254976; ENSG00000132639. [P60880-1]
ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
GeneID6616.
KEGGhsa:6616.
UCSCuc002wnq.2. human.
uc002wnr.2. human. [P60880-2]

Organism-specific databases

CTD6616.
GeneCardsGC20P010199.
HGNCHGNC:11132. SNAP25.
HPACAB000360.
HPA001830.
MIM600322. gene.
neXtProtNX_P60880.
PharmGKBPA35980.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259235.
HOVERGENHBG056971.
KOK08508.
OMAESADAYQ.
OrthoDBEOG75F4F5.
PhylomeDBP60880.
TreeFamTF315125.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.
REACT_116125. Disease.
REACT_13685. Neuronal System.

Gene expression databases

BgeeP60880.
CleanExHS_SNAP25.
GenevestigatorP60880.

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. human.
EvolutionaryTraceP60880.
GeneWikiSNAP25.
GenomeRNAi6616.
NextBio25761.
PMAP-CutDBQ5U0B5.
PROP60880.
SOURCESearch...

Entry information

Entry nameSNP25_HUMAN
AccessionPrimary (citable) accession number: P60880
Secondary accession number(s): B2RAU4 expand/collapse secondary AC list , D3DW16, D3DW17, P13795, P36974, P70557, P70558, Q53EM2, Q5U0B5, 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 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM