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O00161 (SNP23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. 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 23

Short name=SNAP-23
Alternative name(s):
Vesicle-membrane fusion protein SNAP-23
Gene names
Name:SNAP23
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length211 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.

Subunit structure

Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3. Binds simultaneously to SNAPIN and SYN4. Found in a complex with VAMP8 and STX4 in pancreas. Interacts with STX1A and STX12 By similarity. Binds tightly to multiple syntaxins and synaptobrevins/VAMPs. Found in a complex with VAMP8 and STX1A. Ref.9 Ref.18

Subcellular location

Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Cell junctionsynapsesynaptosome. Note: Mainly localized to the plasma membrane.

Tissue specificity

Ubiquitous. Highest levels where found in placenta.

Sequence similarities

Belongs to the SNAP-25 family.

Contains 2 t-SNARE coiled-coil homology domains.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NAPAP549202EBI-745000,EBI-749652

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform SNAP-23a (identifier: O00161-1)

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 SNAP-23b (identifier: O00161-2)

The sequence of this isoform differs from the canonical sequence as follows:
     89-89: R → S
     90-142: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 211211Synaptosomal-associated protein 23
PRO_0000213598

Regions

Domain14 – 7663t-SNARE coiled-coil homology 1
Domain146 – 20863t-SNARE coiled-coil homology 2
Coiled coil23 – 7654 Ref.18

Amino acid modifications

Modified residue11N-acetylmethionine Ref.7 Ref.8 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17
Modified residue201Phosphoserine By similarity
Modified residue231Phosphoserine By similarity
Modified residue341Phosphoserine Ref.15
Modified residue1101Phosphoserine Ref.10 Ref.12 Ref.15
Lipidation791S-palmitoyl cysteine Ref.14
Lipidation801S-palmitoyl cysteine Ref.14
Lipidation831S-palmitoyl cysteine Ref.14
Lipidation851S-palmitoyl cysteine Ref.14
Lipidation871S-palmitoyl cysteine Ref.14
Lipidation1121S-palmitoyl cysteine Ref.14

Natural variations

Alternative sequence891R → S in isoform SNAP-23b.
VSP_006187
Alternative sequence90 – 14253Missing in isoform SNAP-23b.
VSP_006188

Experimental info

Sequence conflict1351A → V in AAC50537. Ref.1

Secondary structure

... 211
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform SNAP-23a [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: AC378E9786C3A239

FASTA21123,354
        10         20         30         40         50         60 
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD 

        70         80         90        100        110        120 
QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK TTWGDGGENS PCNVVSKQPG 

       130        140        150        160        170        180 
PVTNGQLQQP TTGAASGGYI KRITNDARED EMEENLTQVG SILGNLKDMA LNIGNEIDAQ 

       190        200        210 
NPQIKRITDK ADTNRDRIDI ANARAKKLID S 

« Hide

Isoform SNAP-23b [UniParc].

Checksum: 985F775F40884E07
Show »

FASTA15817,789

References

« Hide 'large scale' references
[1]"Identification of a novel syntaxin- and synaptobrevin/VAMP-binding protein, SNAP-23, expressed in non-neuronal tissues."
Ravichandran V., Chawla A., Roche P.A.
J. Biol. Chem. 271:13300-13303(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SNAP-23A).
Tissue: B-cell.
[2]"Identification of two isoforms of the vesicle-membrane fusion protein SNAP-23 in human neutrophils and HL-60 cells."
Mollinedo F., Lazo P.A.
Biochem. Biophys. Res. Commun. 231:808-812(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SNAP-23A AND SNAP-23B).
Tissue: Neutrophil.
[3]"Genomic organization, chromosomal localization, alternative splicing, and isoforms of human Synaptosome associated protein-23 gene implicated in vesicle-membrane fusion."
Lazo P.A., Nadal M., Ferrer M., Area E., Hernandez-Torres J., Nabokina S.M., Mollinedo F., Estivill X.
Hum. Genet. 108:211-215(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
[5]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SNAP-23A).
[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 SNAP-23A).
Tissue: Cervix, Placenta and Testis.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-12, ACETYLATION AT MET-1.
Tissue: Platelet.
[8]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-12 AND 55-64, ACETYLATION AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]"Vesicle-associated membrane protein 3 (VAMP-3) and VAMP-8 are present in human platelets and are required for granule secretion."
Polgar J., Chung S.H., Reed G.L.
Blood 100:1081-1083(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A COMPLEX WITH VAMP8 AND STX1A.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Site-specific analysis of protein S-acylation by resin-assisted capture."
Forrester M.T., Hess D.T., Thompson J.W., Hultman R., Moseley M.A., Stamler J.S., Casey P.J.
J. Lipid Res. 52:393-398(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-79; CYS-80; CYS-83; CYS-85; CYS-87 AND CYS-112.
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Homotetrameric structure of the SNAP-23 N-terminal coiled-coil domain."
Freedman S.J., Song H.K., Xu Y., Sun Z.Y., Eck M.J.
J. Biol. Chem. 278:13462-13467(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 23-76, COILED-COIL DOMAIN, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U55936 mRNA. Translation: AAC50537.1.
Y09567 mRNA. Translation: CAA70760.1.
Y09568 mRNA. Translation: CAA70761.1.
AJ011915 mRNA. Translation: CAA09864.1.
AJ278972, AJ278973, AJ278974 Genomic DNA. Translation: CAC07504.1.
BT006916 mRNA. Translation: AAP35562.1.
CR457212 mRNA. Translation: CAG33493.1.
BC000148 mRNA. Translation: AAH00148.1.
BC003686 mRNA. Translation: AAH03686.1.
BC022890 mRNA. Translation: AAH22890.1.
PIRJC5296.
JC5297.
RefSeqNP_003816.2. NM_003825.3.
NP_570710.1. NM_130798.2.
UniGeneHs.511149.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHLX-ray2.30A23-76[»]
3ZUSX-ray2.95A/B/C/D150-209[»]
ProteinModelPortalO00161.
SMRO00161. Positions 23-76, 147-205.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114303. 49 interactions.
IntActO00161. 14 interactions.
MINTMINT-4999382.
STRING9606.ENSP00000249647.

Protein family/group databases

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

PTM databases

PhosphoSiteO00161.

2D gel databases

OGPO00161.

Proteomic databases

PaxDbO00161.
PRIDEO00161.

Protocols and materials databases

DNASU8773.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000249647; ENSP00000249647; ENSG00000092531. [O00161-1]
ENST00000349777; ENSP00000207062; ENSG00000092531. [O00161-2]
ENST00000397138; ENSP00000380327; ENSG00000092531. [O00161-2]
GeneID8773.
KEGGhsa:8773.
UCSCuc001zpz.2. human. [O00161-1]
uc001zqa.2. human. [O00161-2]

Organism-specific databases

CTD8773.
GeneCardsGC15P042787.
HGNCHGNC:11131. SNAP23.
HPAHPA001214.
MIM602534. gene.
neXtProtNX_O00161.
PharmGKBPA35979.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259235.
HOGENOMHOG000231599.
HOVERGENHBG056971.
InParanoidO00161.
KOK08508.
OMAETRTKNF.
PhylomeDBO00161.
TreeFamTF315125.

Enzyme and pathway databases

ReactomeREACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpressO00161.
BgeeO00161.
CleanExHS_SNAP23.
GenevestigatorO00161.

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

ChiTaRSSNAP23. human.
EvolutionaryTraceO00161.
GeneWikiSNAP23.
GenomeRNAi8773.
NextBio32894.
PMAP-CutDBO00161.
PROO00161.
SOURCESearch...

Entry information

Entry nameSNP23_HUMAN
AccessionPrimary (citable) accession number: O00161
Secondary accession number(s): O00162, Q13602, Q6IAE3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 148 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 15

Human chromosome 15: entries, gene names and cross-references to MIM