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Protein

Synaptosomal-associated protein 25

Gene

SNAP25

Organism
Homo sapiens (Human)
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. 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. Modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1 in pancreatic beta cells.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei180 – 1812Cleavage; by BONT/E

GO - Molecular functioni

  • calcium-dependent protein binding Source: ParkinsonsUK-UCL
  • SNAP receptor activity Source: GO_Central
  • syntaxin-1 binding Source: UniProtKB

GO - Biological processi

  • associative learning Source: Ensembl
  • energy reserve metabolic process Source: Reactome
  • glutamate secretion Source: Reactome
  • locomotory behavior Source: Ensembl
  • long-term synaptic potentiation Source: Ensembl
  • neurotransmitter secretion Source: Reactome
  • neurotransmitter uptake Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of neuron projection development Source: Ensembl
  • small molecule metabolic process Source: Reactome
  • synaptic transmission Source: UniProtKB
  • synaptic vesicle docking Source: UniProtKB
  • synaptic vesicle exocytosis Source: ParkinsonsUK-UCL
  • synaptic vesicle fusion to presynaptic membrane Source: GO_Central
  • synaptic vesicle priming Source: GO_Central
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_18325. Regulation of insulin secretion.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_263969. Toxicity of botulinum toxin type C (BoNT/C).
REACT_264227. Toxicity of botulinum toxin type E (BoNT/E).
REACT_264537. Toxicity of botulinum toxin type A (BoNT/A).

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:11132. SNAP25.

Subcellular locationi

  • Cytoplasmperinuclear region By similarity
  • Cell membrane By similarity; Lipid-anchor
  • Cell junctionsynapsesynaptosome

  • Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region. Colocalizes with KCNB1 at the cell membrane (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35980.

Chemistry

DrugBankiDB00083. Botulinum Toxin Type A.

Polymorphism and mutation databases

BioMutaiSNAP25.
DMDMi46397726.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 206206Synaptosomal-associated protein 25PRO_0000213587Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi85 – 851S-palmitoyl cysteineBy similarity
Lipidationi88 – 881S-palmitoyl cysteineBy similarity
Lipidationi90 – 901S-palmitoyl cysteineBy similarity
Lipidationi92 – 921S-palmitoyl cysteineBy similarity
Modified residuei138 – 1381PhosphothreonineBy similarity
Modified residuei187 – 1871PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiP60880.
PaxDbiP60880.
PRIDEiP60880.

PTM databases

PhosphoSiteiP60880.

Miscellaneous databases

PMAP-CutDBQ5U0B5.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP60880.
CleanExiHS_SNAP25.
ExpressionAtlasiP60880. baseline and differential.
GenevisibleiP60880. HS.

Organism-specific databases

HPAiCAB000360.
HPA001830.

Interactioni

Subunit structurei

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. Interacts with KCNB1 (via N-terminus); reduces the voltage-dependent potassium channel KCNB1 activity in pancreatic beta cell. Interacts with ZDHHC13 (via ANK repeats). Interacts with ZDHHC17 (via ANK repeats) (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
ZDHHC17Q8IUH53EBI-524785,EBI-524753

Protein-protein interaction databases

BioGridi112500. 30 interactions.
DIPiDIP-34554N.
IntActiP60880. 11 interactions.
MINTiMINT-1403389.
STRINGi9606.ENSP00000254976.

Structurei

Secondary structure

1
206
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi8 – 8073Combined sources
Helixi148 – 16720Combined sources
Beta strandi191 – 1933Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30C10-81[»]
D139-204[»]
1XTGX-ray2.10B146-204[»]
2N1TNMR-C7-83[»]
D131-204[»]
3DDAX-ray1.50B197-202[»]
3DDBX-ray1.60B198-202[»]
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[»]
ProteinModelPortaliP60880.
SMRiP60880. Positions 10-78, 141-204.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60880.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini19 – 8163t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
BLAST
Domaini140 – 20263t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7575Interaction with CENPFBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi85 – 928Cys-rich

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

eggNOGiNOG259235.
GeneTreeiENSGT00390000012186.
HOVERGENiHBG056971.
InParanoidiP60880.
KOiK18211.
OMAiDNAWKAN.
OrthoDBiEOG75F4F5.
PhylomeDBiP60880.
TreeFamiTF315125.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 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: P60880-1) [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: P60880-2) [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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti44 – 441I → V in BAD97337 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 8932ERIEE…CGLCV → DRVEEGMNHINQDMKEAEKN LKDLGKCCGLFI in isoform 2. 5 PublicationsVSP_006186Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13109.1. [P60880-2]
CCDS13110.1.
PIRiI53735.
I67823.
RefSeqiNP_003072.2. NM_003081.3. [P60880-2]
NP_570824.1. NM_130811.2. [P60880-1]
XP_005260865.1. XM_005260808.3. [P60880-1]
XP_005260867.1. XM_005260810.3. [P60880-2]
UniGeneiHs.167317.

Genome annotation databases

EnsembliENST00000254976; ENSP00000254976; ENSG00000132639.
ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
GeneIDi6616.
KEGGihsa:6616.
UCSCiuc002wnq.2. human.
uc002wnr.2. human. [P60880-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS13109.1. [P60880-2]
CCDS13110.1.
PIRiI53735.
I67823.
RefSeqiNP_003072.2. NM_003081.3. [P60880-2]
NP_570824.1. NM_130811.2. [P60880-1]
XP_005260865.1. XM_005260808.3. [P60880-1]
XP_005260867.1. XM_005260810.3. [P60880-2]
UniGeneiHs.167317.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KILX-ray2.30C10-81[»]
D139-204[»]
1XTGX-ray2.10B146-204[»]
2N1TNMR-C7-83[»]
D131-204[»]
3DDAX-ray1.50B197-202[»]
3DDBX-ray1.60B198-202[»]
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[»]
ProteinModelPortaliP60880.
SMRiP60880. Positions 10-78, 141-204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112500. 30 interactions.
DIPiDIP-34554N.
IntActiP60880. 11 interactions.
MINTiMINT-1403389.
STRINGi9606.ENSP00000254976.

Chemistry

ChEMBLiCHEMBL2364159.
DrugBankiDB00083. Botulinum Toxin Type A.

Protein family/group databases

TCDBi1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteiP60880.

Polymorphism and mutation databases

BioMutaiSNAP25.
DMDMi46397726.

Proteomic databases

MaxQBiP60880.
PaxDbiP60880.
PRIDEiP60880.

Protocols and materials databases

DNASUi6616.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254976; ENSP00000254976; ENSG00000132639.
ENST00000304886; ENSP00000307341; ENSG00000132639. [P60880-2]
GeneIDi6616.
KEGGihsa:6616.
UCSCiuc002wnq.2. human.
uc002wnr.2. human. [P60880-2]

Organism-specific databases

CTDi6616.
GeneCardsiGC20P010199.
HGNCiHGNC:11132. SNAP25.
HPAiCAB000360.
HPA001830.
MIMi600322. gene.
neXtProtiNX_P60880.
PharmGKBiPA35980.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG259235.
GeneTreeiENSGT00390000012186.
HOVERGENiHBG056971.
InParanoidiP60880.
KOiK18211.
OMAiDNAWKAN.
OrthoDBiEOG75F4F5.
PhylomeDBiP60880.
TreeFamiTF315125.

Enzyme and pathway databases

ReactomeiREACT_12591. Glutamate Neurotransmitter Release Cycle.
REACT_15293. Dopamine Neurotransmitter Release Cycle.
REACT_15309. Acetylcholine Neurotransmitter Release Cycle.
REACT_15418. Norepinephrine Neurotransmitter Release Cycle.
REACT_15425. Serotonin Neurotransmitter Release Cycle.
REACT_18325. Regulation of insulin secretion.
REACT_23947. GABA synthesis, release, reuptake and degradation.
REACT_263969. Toxicity of botulinum toxin type C (BoNT/C).
REACT_264227. Toxicity of botulinum toxin type E (BoNT/E).
REACT_264537. Toxicity of botulinum toxin type A (BoNT/A).

Miscellaneous databases

ChiTaRSiSNAP25. human.
EvolutionaryTraceiP60880.
GeneWikiiSNAP25.
GenomeRNAii6616.
NextBioi25761.
PMAP-CutDBQ5U0B5.
PROiP60880.
SOURCEiSearch...

Gene expression databases

BgeeiP60880.
CleanExiHS_SNAP25.
ExpressionAtlasiP60880. baseline and differential.
GenevisibleiP60880. HS.

Family and domain databases

InterProiIPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view]
PfamiPF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view]
SMARTiSM00397. t_SNARE. 2 hits.
[Graphical view]
PROSITEiPS50192. T_SNARE. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiSNP25_HUMAN
AccessioniPrimary (citable) accession number: P60880
Secondary accession number(s): B2RAU4
, D3DW16, D3DW17, P13795, P36974, P70557, P70558, Q53EM2, Q5U0B5, Q8IXK3, Q96FM2, Q9BR45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: April 13, 2004
Last modified: July 22, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.