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O00161

- SNP23_HUMAN

UniProt

O00161 - SNP23_HUMAN

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Protein

Synaptosomal-associated protein 23

Gene

SNAP23

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Biological processi

  1. exocytosis Source: Ensembl
  2. membrane fusion Source: ProtInc
  3. membrane organization Source: Reactome
  4. post-Golgi vesicle-mediated transport Source: Reactome
  5. protein transport Source: UniProtKB-KW
  6. vesicle targeting Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_19187. Clathrin derived vesicle budding.

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 23
Short name:
SNAP-23
Alternative name(s):
Vesicle-membrane fusion protein SNAP-23
Gene namesi
Name:SNAP23
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:11131. SNAP23.

Subcellular locationi

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

GO - Cellular componenti

  1. azurophil granule Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. focal adhesion Source: UniProtKB
  4. neuron projection Source: UniProtKB-KW
  5. nucleus Source: HPA
  6. plasma membrane Source: HPA
  7. specific granule Source: UniProtKB
  8. synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35979.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 211211Synaptosomal-associated protein 23PRO_0000213598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine7 Publications
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei34 – 341Phosphoserine1 Publication
Lipidationi79 – 791S-palmitoyl cysteine1 Publication
Lipidationi80 – 801S-palmitoyl cysteine1 Publication
Lipidationi83 – 831S-palmitoyl cysteine1 Publication
Lipidationi85 – 851S-palmitoyl cysteine1 Publication
Lipidationi87 – 871S-palmitoyl cysteine1 Publication
Modified residuei110 – 1101Phosphoserine3 Publications
Lipidationi112 – 1121S-palmitoyl cysteine1 Publication

Keywords - PTMi

Acetylation, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

MaxQBiO00161.
PaxDbiO00161.
PRIDEiO00161.

2D gel databases

OGPiO00161.

PTM databases

PhosphoSiteiO00161.

Miscellaneous databases

PMAP-CutDBO00161.

Expressioni

Tissue specificityi

Ubiquitous. Highest levels where found in placenta.

Gene expression databases

BgeeiO00161.
CleanExiHS_SNAP23.
ExpressionAtlasiO00161. baseline and differential.
GenevestigatoriO00161.

Organism-specific databases

HPAiHPA001214.

Interactioni

Subunit structurei

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.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NAPAP549202EBI-745000,EBI-749652
ZDHHC17Q8IUH54EBI-745000,EBI-524753

Protein-protein interaction databases

BioGridi114303. 51 interactions.
IntActiO00161. 15 interactions.
MINTiMINT-4999382.
STRINGi9606.ENSP00000249647.

Structurei

Secondary structure

1
211
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 7451Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1NHLX-ray2.30A23-76[»]
3ZUSX-ray2.95A/B/C/D150-211[»]
ProteinModelPortaliO00161.
SMRiO00161. Positions 23-76, 147-205.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00161.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini14 – 7663t-SNARE coiled-coil homology 1PROSITE-ProRule annotationAdd
BLAST
Domaini146 – 20863t-SNARE coiled-coil homology 2PROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili23 – 76541 PublicationAdd
BLAST

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.
HOGENOMiHOG000231599.
HOVERGENiHBG056971.
InParanoidiO00161.
KOiK08508.
OMAiCPCNRFS.
PhylomeDBiO00161.
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. Align

Isoform SNAP-23a (identifier: O00161-1) [UniParc]FASTAAdd to Basket

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
MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE
60 70 80 90 100
QLNRIEEGLD QINKDMRETE KTLTELNKCC GLCVCPCNRT KNFESGKAYK
110 120 130 140 150
TTWGDGGENS PCNVVSKQPG PVTNGQLQQP TTGAASGGYI KRITNDARED
160 170 180 190 200
EMEENLTQVG SILGNLKDMA LNIGNEIDAQ NPQIKRITDK ADTNRDRIDI
210
ANARAKKLID S
Length:211
Mass (Da):23,354
Last modified:July 1, 1997 - v1
Checksum:iAC378E9786C3A239
GO
Isoform SNAP-23b (identifier: O00161-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:158
Mass (Da):17,789
Checksum:i985F775F40884E07
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti135 – 1351A → V in AAC50537. (PubMed:8663154)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 891R → S in isoform SNAP-23b. 1 PublicationVSP_006187
Alternative sequencei90 – 14253Missing in isoform SNAP-23b. 1 PublicationVSP_006188Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS10087.1. [O00161-1]
CCDS10088.1. [O00161-2]
PIRiJC5296.
JC5297.
RefSeqiNP_003816.2. NM_003825.3. [O00161-1]
NP_570710.1. NM_130798.2. [O00161-2]
UniGeneiHs.511149.

Genome annotation databases

EnsembliENST00000249647; ENSP00000249647; ENSG00000092531. [O00161-1]
ENST00000349777; ENSP00000207062; ENSG00000092531. [O00161-2]
ENST00000397138; ENSP00000380327; ENSG00000092531. [O00161-2]
GeneIDi8773.
KEGGihsa:8773.
UCSCiuc001zpz.2. human. [O00161-1]
uc001zqa.2. human. [O00161-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS10087.1. [O00161-1 ]
CCDS10088.1. [O00161-2 ]
PIRi JC5296.
JC5297.
RefSeqi NP_003816.2. NM_003825.3. [O00161-1 ]
NP_570710.1. NM_130798.2. [O00161-2 ]
UniGenei Hs.511149.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1NHL X-ray 2.30 A 23-76 [» ]
3ZUS X-ray 2.95 A/B/C/D 150-211 [» ]
ProteinModelPortali O00161.
SMRi O00161. Positions 23-76, 147-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114303. 51 interactions.
IntActi O00161. 15 interactions.
MINTi MINT-4999382.
STRINGi 9606.ENSP00000249647.

Protein family/group databases

TCDBi 1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSitei O00161.

2D gel databases

OGPi O00161.

Proteomic databases

MaxQBi O00161.
PaxDbi O00161.
PRIDEi O00161.

Protocols and materials databases

DNASUi 8773.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000249647 ; ENSP00000249647 ; ENSG00000092531 . [O00161-1 ]
ENST00000349777 ; ENSP00000207062 ; ENSG00000092531 . [O00161-2 ]
ENST00000397138 ; ENSP00000380327 ; ENSG00000092531 . [O00161-2 ]
GeneIDi 8773.
KEGGi hsa:8773.
UCSCi uc001zpz.2. human. [O00161-1 ]
uc001zqa.2. human. [O00161-2 ]

Organism-specific databases

CTDi 8773.
GeneCardsi GC15P042787.
HGNCi HGNC:11131. SNAP23.
HPAi HPA001214.
MIMi 602534. gene.
neXtProti NX_O00161.
PharmGKBi PA35979.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG259235.
GeneTreei ENSGT00390000012186.
HOGENOMi HOG000231599.
HOVERGENi HBG056971.
InParanoidi O00161.
KOi K08508.
OMAi CPCNRFS.
PhylomeDBi O00161.
TreeFami TF315125.

Enzyme and pathway databases

Reactomei REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_19187. Clathrin derived vesicle budding.

Miscellaneous databases

ChiTaRSi SNAP23. human.
EvolutionaryTracei O00161.
GeneWikii SNAP23.
GenomeRNAii 8773.
NextBioi 32894.
PMAP-CutDB O00161.
PROi O00161.
SOURCEi Search...

Gene expression databases

Bgeei O00161.
CleanExi HS_SNAP23.
ExpressionAtlasi O00161. baseline and differential.
Genevestigatori O00161.

Family and domain databases

InterProi IPR000928. SNAP-25.
IPR000727. T_SNARE_dom.
[Graphical view ]
Pfami PF00835. SNAP-25. 1 hit.
PF05739. SNARE. 1 hit.
[Graphical view ]
SMARTi SM00397. t_SNARE. 2 hits.
[Graphical view ]
PROSITEi PS50192. T_SNARE. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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.

Entry informationi

Entry nameiSNP23_HUMAN
AccessioniPrimary (citable) accession number: O00161
Secondary accession number(s): O00162, Q13602, Q6IAE3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 154 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

Keywords - Technical termi

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

Documents

  1. Human chromosome 15
    Human chromosome 15: 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