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Protein

Synaptosomal-associated protein 25

Gene

Snap25

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

t-SNARE involved in the molecular regulation of neurotransmitter release. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells (PubMed:12403834). 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.1 Publication

GO - Molecular functioni

  • calcium-dependent protein binding Source: ParkinsonsUK-UCL
  • ion channel binding Source: UniProtKB
  • myosin binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein N-terminus binding Source: RGD
  • SNAP receptor activity Source: RGD
  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: RGD
  • voltage-gated potassium channel activity Source: RGD

GO - Biological processi

  • axonogenesis Source: RGD
  • calcium ion-regulated exocytosis of neurotransmitter Source: RGD
  • endosomal transport Source: RGD
  • exocytosis Source: RGD
  • growth hormone secretion Source: RGD
  • long-term memory Source: RGD
  • positive regulation of hormone secretion Source: RGD
  • positive regulation of insulin secretion Source: RGD
  • regulation of neuron projection development Source: ParkinsonsUK-UCL
  • regulation of synapse assembly Source: RGD
  • sleep Source: RGD
  • synaptic vesicle fusion to presynaptic active zone membrane Source: GO_Central
  • synaptic vesicle priming Source: GO_Central
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptosomal-associated protein 25
Short name:
SNAP-25
Alternative name(s):
Super protein
Short name:
SUP
Synaptosomal-associated 25 kDa protein
Gene namesi
Name:Snap25
Synonyms:Snap
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3728. Snap25.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: RGD
  • axon Source: MGI
  • axonal growth cone Source: MGI
  • cell junction Source: UniProtKB-KW
  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • endosome Source: RGD
  • filopodium Source: RGD
  • growth cone Source: HGNC
  • intracellular organelle Source: RGD
  • lamellipodium Source: RGD
  • membrane Source: UniProtKB
  • membrane raft Source: RGD
  • neuronal cell body Source: RGD
  • neuron projection Source: HGNC
  • perinuclear region of cytoplasm Source: UniProtKB-SubCell
  • plasma membrane Source: ParkinsonsUK-UCL
  • SNARE complex Source: HGNC
  • synaptobrevin 2-SNAP-25-syntaxin-1a complex Source: RGD
  • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex Source: MGI
  • synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex Source: RGD
  • terminal bouton Source: ParkinsonsUK-UCL
  • voltage-gated potassium channel complex Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi113V → A: Inhibits interaction with ZDHHC13 and ZDHHC17. 1 Publication1
Mutagenesisi116Q → A: Inhibits interaction with ZDHHC13 and ZDHHC17. 1 Publication1
Mutagenesisi117P → A: Inhibits interaction with ZDHHC13 and ZDHHC17. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1075243.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002135921 – 206Synaptosomal-associated protein 25Add BLAST206

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi85S-palmitoyl cysteineBy similarity1
Lipidationi88S-palmitoyl cysteineBy similarity1
Lipidationi90S-palmitoyl cysteineBy similarity1
Lipidationi92S-palmitoyl cysteineBy similarity1
Modified residuei138Phosphothreonine; by PKC and PKA1 Publication1
Modified residuei154PhosphoserineBy similarity1
Modified residuei187Phosphoserine; by PKC1 Publication1

Post-translational modificationi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei180 – 181Cleavage; by BONT/EBy similarity2

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PRIDEiP60881.

2D gel databases

World-2DPAGE0004:P60881.

PTM databases

iPTMnetiP60881.
PhosphoSitePlusiP60881.
SwissPalmiP60881.

Miscellaneous databases

PMAP-CutDBP60881.

Expressioni

Gene expression databases

BgeeiENSRNOG00000006037.

Interactioni

Subunit structurei

Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A; this complex binds CPLX1 (PubMed:9759724, PubMed:12496247). Found in a complex containing SYT1, SV2B and syntaxin-1 (By similarity). Found in a ternary complex with STX1A and VAMP8 (PubMed:10336434). Isoform 1 and isoform 2 interact with BLOC1S6 (By similarity). Interacts with CENPF (By similarity). Interacts with EQTN (By similarity). Interacts with HGS (PubMed:9039916). Interacts with KCNB1 (via N-terminus); reduces the voltage-dependent potassium channel KCNB1 activity in pancreatic beta cells (PubMed:12403834). Interacts with OTOF (By similarity). Interacts with RIMS1 (PubMed:11438518). Interacts with SNAPIN (By similarity). Interacts with STXBP6 (PubMed:12145319). Interacts with TRIM9 (By similarity). Interacts with ZDHHC13 (via ANK repeats) (PubMed:26198635). Interacts with ZDHHC17 (via ANK repeats) (PubMed:26198635). Associates with the BLOC-1 complex (By similarity).By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Rph3aP477094EBI-1027214,EBI-1027524
Srcin1Q9QXY23EBI-1027214,EBI-1394088
Stx1aP3285110EBI-1027214,EBI-539720

GO - Molecular functioni

  • calcium-dependent protein binding Source: ParkinsonsUK-UCL
  • ion channel binding Source: UniProtKB
  • myosin binding Source: RGD
  • protein domain specific binding Source: RGD
  • protein N-terminus binding Source: RGD
  • SNAP receptor activity Source: RGD
  • SNARE binding Source: RGD
  • syntaxin-1 binding Source: RGD

Protein-protein interaction databases

BioGridi247095. 10 interactors.
DIPiDIP-29205N.
IntActiP60881. 17 interactors.
MINTiMINT-95953.

Structurei

Secondary structure

1206
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 82Combined sources76
Helixi142 – 201Combined sources60

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JTHX-ray2.00A/C1-82[»]
1N7SX-ray1.45C7-83[»]
D141-204[»]
1SFCX-ray2.40C/G/K1-83[»]
D/H/L120-206[»]
1URQX-ray2.00C7-83[»]
D142-204[»]
3HD7X-ray3.40C/G7-83[»]
D/H141-204[»]
3IPDX-ray4.80C/G7-83[»]
D/H141-204[»]
3J96electron microscopy7.60M17-204[»]
3J97electron microscopy7.80M7-204[»]
3J98electron microscopy8.40M17-204[»]
3J99electron microscopy8.20M17-204[»]
5CCGX-ray3.50C/I7-83[»]
D/J141-204[»]
5CCHX-ray3.60C7-83[»]
D141-204[»]
5CCIX-ray4.10C7-83[»]
D141-204[»]
5KJ7X-ray3.50C/I9-83[»]
D/J141-204[»]
5KJ8X-ray4.10C/I9-83[»]
D/J141-204[»]
DisProtiDP00068.
ProteinModelPortaliP60881.
SMRiP60881.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60881.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini19 – 81t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd BLAST63
Domaini140 – 202t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd BLAST63

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 75Interaction with CENPFBy similarityAdd BLAST75
Regioni111 – 120Interaction with ZDHHC13 and ZDHHC171 Publication10

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi85 – 92Cys-rich8

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 2 t-SNARE coiled-coil homology domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat

Phylogenomic databases

HOVERGENiHBG056971.
InParanoidiP60881.
KOiK18211.
PhylomeDBiP60881.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

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: P60881-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MAEDADMRNE LEEMQRRADQ LADESLESTR RMLQLVEESK DAGIRTLVML
60 70 80 90 100
DEQGEQLERI EEGMDQINKD MKEAEKNLTD LGKFCGLCVC PCNKLKSSDA
110 120 130 140 150
YKKAWGNNQD GVVASQPARV VDEREQMAIS GGFIRRVTND ARENEMDENL
160 170 180 190 200
EQVSGIIGNL RHMALDMGNE IDTQNRQIDR IMEKADSNKT RIDEANQRAT

KMLGSG
Length:206
Mass (Da):23,315
Last modified:April 13, 2004 - v1
Checksum:iFBED2B082A4CB6A6
GO
Isoform 2 (identifier: P60881-2) [UniParc] [UniParc]FASTAAdd to basket
Also known as: SNAP-25a

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

Show »
Length:206
Mass (Da):23,336
Checksum:iE272652C701EA984
GO

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01002058 – 89ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2. 2 PublicationsAdd BLAST32

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003991 mRNA. Translation: BAA20151.1.
AB003992 mRNA. Translation: BAA20152.1.
AF245227 mRNA. Translation: AAF81202.1.
U56262 mRNA. Translation: AAA99826.1.
BC087699 mRNA. Translation: AAH87699.1.
U56261 mRNA. Translation: AAA99825.1.
RefSeqiNP_001257504.1. NM_001270575.1. [P60881-2]
NP_001257505.1. NM_001270576.1. [P60881-2]
NP_112253.1. NM_030991.3. [P60881-1]
UniGeneiRn.107689.

Genome annotation databases

GeneIDi25012.
KEGGirno:25012.
UCSCiRGD:3728. rat.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB003991 mRNA. Translation: BAA20151.1.
AB003992 mRNA. Translation: BAA20152.1.
AF245227 mRNA. Translation: AAF81202.1.
U56262 mRNA. Translation: AAA99826.1.
BC087699 mRNA. Translation: AAH87699.1.
U56261 mRNA. Translation: AAA99825.1.
RefSeqiNP_001257504.1. NM_001270575.1. [P60881-2]
NP_001257505.1. NM_001270576.1. [P60881-2]
NP_112253.1. NM_030991.3. [P60881-1]
UniGeneiRn.107689.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JTHX-ray2.00A/C1-82[»]
1N7SX-ray1.45C7-83[»]
D141-204[»]
1SFCX-ray2.40C/G/K1-83[»]
D/H/L120-206[»]
1URQX-ray2.00C7-83[»]
D142-204[»]
3HD7X-ray3.40C/G7-83[»]
D/H141-204[»]
3IPDX-ray4.80C/G7-83[»]
D/H141-204[»]
3J96electron microscopy7.60M17-204[»]
3J97electron microscopy7.80M7-204[»]
3J98electron microscopy8.40M17-204[»]
3J99electron microscopy8.20M17-204[»]
5CCGX-ray3.50C/I7-83[»]
D/J141-204[»]
5CCHX-ray3.60C7-83[»]
D141-204[»]
5CCIX-ray4.10C7-83[»]
D141-204[»]
5KJ7X-ray3.50C/I9-83[»]
D/J141-204[»]
5KJ8X-ray4.10C/I9-83[»]
D/J141-204[»]
DisProtiDP00068.
ProteinModelPortaliP60881.
SMRiP60881.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247095. 10 interactors.
DIPiDIP-29205N.
IntActiP60881. 17 interactors.
MINTiMINT-95953.

Chemistry databases

ChEMBLiCHEMBL1075243.

PTM databases

iPTMnetiP60881.
PhosphoSitePlusiP60881.
SwissPalmiP60881.

2D gel databases

World-2DPAGE0004:P60881.

Proteomic databases

PRIDEiP60881.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25012.
KEGGirno:25012.
UCSCiRGD:3728. rat.

Organism-specific databases

CTDi6616.
RGDi3728. Snap25.

Phylogenomic databases

HOVERGENiHBG056971.
InParanoidiP60881.
KOiK18211.
PhylomeDBiP60881.

Miscellaneous databases

EvolutionaryTraceiP60881.
PMAP-CutDBP60881.
PROiP60881.

Gene expression databases

BgeeiENSRNOG00000006037.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSNP25_RAT
AccessioniPrimary (citable) accession number: P60881
Secondary accession number(s): P13795
, P36974, P70557, P70558, Q8IXK3, Q96FM2, Q9BR45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: November 30, 2016
This is version 139 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.