P60880 (SNP25_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	206 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › perinuclear region By similarity. Cell membrane; Lipid-anchor. Cell junction › synapse › synaptosome. 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 component	Cell junction Cell membrane Cytoplasm Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	energy reserve metabolic process Traceable author statement. Source: Reactome glutamate 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 vesicle docking involved in exocytosis Non-traceable author statement Ref.3. Source: UniProtKB
Cellular_component	SNARE complex Inferred from direct assay PubMed 19546860. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW growth cone 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: Compara trans-Golgi network Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ZDHHC17	Q8IUH5	3	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 206

206

Synaptosomal-associated protein 25

PRO_0000213587

Regions

Domain

19 – 81

63

t-SNARE coiled-coil homology 1

Domain

140 – 202

63

t-SNARE coiled-coil homology 2

Region

1 – 75

75

Interaction with CENPF By similarity

Compositional bias

85 – 92

8

Cys-rich

Sites

Site

180 – 181

2

Cleavage; by BONT/E

Amino acid modifications

Modified residue

138

1

Phosphothreonine By similarity

Modified residue

187

1

Phosphoserine By similarity

Lipidation

85

1

S-palmitoyl cysteine By similarity

Lipidation

88

1

S-palmitoyl cysteine By similarity

Lipidation

90

1

S-palmitoyl cysteine By similarity

Lipidation

92

1

S-palmitoyl cysteine By similarity

Natural variations

Alternative sequence

58 – 89

32

ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2.

VSP_006186

Experimental info

Sequence conflict

44

1

I → V in BAD97337. Ref.5

Secondary structure

1

.

.

.

.

.

206

Helix Strand Turn

Details...

Helix

148 – 167

20

Beta strand

191 – 193

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (SNAP-25b) [UniParc]. Last modified April 13, 2004. Version 1. Checksum: FBED2B082A4CB6A6	FASTA	206	23,315
	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
	Isoform 2 (SNAP-25a) [UniParc] [UniParc]. Checksum: E272652C701EA984	FASTA	206	23,336
	10 20 30 40 50 60 MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML DEQGEQLDRV 70 80 90 100 110 120 EEGMNHINQD MKEAEKNLKD LGKCCGLFIC PCNKLKSSDA YKKAWGNNQD GVVASQPARV 130 140 150 160 170 180 VDEREQMAIS GGFIRRVTND ARENEMDENL EQVSGIIGNL RHMALDMGNE IDTQNRQIDR 190 200 IMEKADSNKT RIDEANQRAT KMLGSG

References

	« Hide 'large scale' referencesShow '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. , 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]	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. , 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.

IPI

IPI00010470.
IPI00107625.

PIR

I53735.
I67823.

RefSeq

NP_003072.2. NM_003081.3.
NP_570824.1. NM_130811.2.

UniGene

Hs.167317.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1KIL	X-ray	2.30	C	11-81	[»]
			D	141-203	[»]
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	[»]

ProteinModelPortal

P60880.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-34554N.

IntAct

P60880. 9 interactions.

MINT

MINT-1403389.

Protein family/group databases

TCDB

1.F.1.1.1. synaptosomal vesicle fusion pore (SVF-Pore) family.

PTM databases

PhosphoSite

P60880.

Polymorphism databases

DMDM

46397726.

Proteomic databases

PaxDb

P60880.

PRIDE

P60880.

Protocols and materials databases

DNASU

6616.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254976; ENSP00000254976; ENSG00000132639.
ENST00000304886; ENSP00000307341; ENSG00000132639.
ENST00000430336; ENSP00000400720; ENSG00000132639.

GeneID

6616.

KEGG

hsa:6616.

UCSC

uc002wnq.2. human.
uc002wnr.2. human.

Organism-specific databases

CTD

6616.

GeneCards

GC20P010199.

HGNC

HGNC:11132. SNAP25.

HPA

CAB000360.
HPA001830.

MIM

600322. gene.

neXtProt

NX_P60880.

PharmGKB

PA35980.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG259235.

HOVERGEN

HBG056971.

KO

K08508.

OMA

ESADAYQ.

OrthoDB

EOG4X3H29.

PhylomeDB

P60880.

Enzyme and pathway databases

Pathway_Interaction_DB

botulinumtoxinpathway. Effects of Botulinum toxin.

Reactome

REACT_111217. Metabolism.
REACT_116125. Disease.
REACT_13685. Neuronal System.

Gene expression databases

Bgee

P60880.

CleanEx

HS_SNAP25.

Genevestigator

P60880.

GermOnline

ENSG00000132639. Homo sapiens.

Family and domain databases

InterPro

IPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]

Pfam

PF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]

SMART

SM00397. t_SNARE. 2 hits.
[Graphical view]

PROSITE

PS50192. T_SNARE. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

SNAP25. human.

DrugBank

DB00083. Botulinum Toxin Type A.

EvolutionaryTrace

P60880.

GenomeRNAi

6616.

NextBio

25761.

PMAP-CutDB

Q5U0B5.

SOURCE

Search...

Entry information

Entry name

SNP25_HUMAN

Accession

Primary (citable) accession number: P60880
Secondary accession number(s): B2RAU4 , 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:	May 29, 2013
This is version 107 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.