O00161 (SNP23_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Synaptosomal-associated protein 23
Short name=SNAP-23

Alternative name(s):
Vesicle-membrane fusion protein SNAP-23

Gene names

Name:

SNAP23

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	211 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15
Subcellular location	Cell membrane; Peripheral membrane protein. Cell membrane; Lipid-anchor. Cell junction › synapse › synaptosome. 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.

Ontologies

Keywords
Biological process	Protein transport Transport
Cellular component	Cell junction Cell membrane Membrane Synapse Synaptosome
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat
PTM	Acetylation Lipoprotein Palmitate Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cellular membrane fusion Traceable author statement PubMed 10839363. Source: ProtInc exocytosis Inferred from electronic annotation. Source: Compara post-Golgi vesicle-mediated transport Traceable author statement. Source: Reactome protein transport Inferred from electronic annotation. Source: UniProtKB-KW vesicle targeting Traceable author statement Ref.1. Source: ProtInc
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA azurophil granule Inferred from direct assay PubMed 18588921. Source: UniProtKB cell junction Inferred from electronic annotation. Source: UniProtKB-KW neuron projection Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay. Source: HPA plasma membrane Inferred from direct assay. Source: HPA specific granule Inferred from direct assay PubMed 18588921. Source: UniProtKB synapse Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NAPA	P54920	2	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 211

211

Synaptosomal-associated protein 23

PRO_0000213598

Regions

Domain

14 – 76

63

t-SNARE coiled-coil homology 1

Domain

146 – 208

63

t-SNARE coiled-coil homology 2

Coiled coil

23 – 76

54

Ref.15

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.7 Ref.8 Ref.11 Ref.14

Modified residue

20

1

Phosphoserine By similarity

Modified residue

34

1

Phosphoserine Ref.14

Modified residue

110

1

Phosphoserine Ref.10 Ref.11 Ref.14

Lipidation

79

1

S-palmitoyl cysteine Ref.13

Lipidation

80

1

S-palmitoyl cysteine Ref.13

Lipidation

83

1

S-palmitoyl cysteine Ref.13

Lipidation

85

1

S-palmitoyl cysteine Ref.13

Lipidation

87

1

S-palmitoyl cysteine Ref.13

Lipidation

112

1

S-palmitoyl cysteine Ref.13

Natural variations

Alternative sequence

89

1

R → S in isoform SNAP-23b.

VSP_006187

Alternative sequence

90 – 142

53

Missing in isoform SNAP-23b.

VSP_006188

Experimental info

Sequence conflict

135

1

A → V in AAC50537. Ref.1

Secondary structure

1

.

.

.

211

Helix Strand Turn

Details...

Helix

24 – 74

51

Sequences

	Sequence		Length	Mass (Da)
	Isoform SNAP-23a [UniParc]. Last modified July 1, 1997. Version 1. Checksum: AC378E9786C3A239	FASTA	211	23,354
	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
	Isoform SNAP-23b [UniParc]. Checksum: 985F775F40884E07	FASTA	158	17,789
	10 20 30 40 50 60 MDNLSSEEIQ QRAHQITDES LESTRRILGL AIESQDAGIK TITMLDEQKE QLNRIEEGLD 70 80 90 100 110 120 QINKDMRETE KTLTELNKCC GLCVCPCNSI TNDAREDEME ENLTQVGSIL GNLKDMALNI 130 140 150 GNEIDAQNPQ IKRITDKADT NRDRIDIANA RAKKLIDS

References

	« Hide 'large scale' referencesShow '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, 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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].
[13]	"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.
[14]	"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, MASS SPECTROMETRY.
[15]	"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 REGION, 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.

IPI

IPI00010438.
IPI00216231.

PIR

JC5296.
JC5297.

RefSeq

NP_003816.2. NM_003825.3.
NP_570710.1. NM_130798.2.

UniGene

Hs.728237.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1NHL	X-ray	2.30	A	23-76	[»]

ProteinModelPortal

O00161.

ModBase

Search...

Protein-protein interaction databases

IntAct

O00161. 11 interactions.

MINT

MINT-4999382.

STRING

9606.ENSP00000249647.

Protein family/group databases

TCDB

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

PTM databases

PhosphoSite

O00161.

2D gel databases

OGP

O00161.

Proteomic databases

PaxDb

O00161.

PRIDE

O00161.

Protocols and materials databases

DNASU

8773.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000249647; ENSP00000249647; ENSG00000092531.
ENST00000349777; ENSP00000207062; ENSG00000092531.
ENST00000397138; ENSP00000380327; ENSG00000092531.

GeneID

8773.

KEGG

hsa:8773.

UCSC

uc001zpz.2. human.
uc001zqa.2. human.

Organism-specific databases

CTD

8773.

GeneCards

GC15P042787.

HGNC

HGNC:11131. SNAP23.

HPA

HPA001214.

MIM

602534. gene.

neXtProt

NX_O00161.

PharmGKB

PA35979.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG259235.

HOGENOM

HOG000231599.

HOVERGEN

HBG056971.

InParanoid

O00161.

KO

K08508.

OMA

EIDKQNK.

OrthoDB

EOG4H9XMG.

PhylomeDB

O00161.

Enzyme and pathway databases

Reactome

REACT_11123. Membrane Trafficking.

Gene expression databases

ArrayExpress

O00161.

Bgee

O00161.

CleanEx

HS_SNAP23.

Genevestigator

O00161.

GermOnline

ENSG00000092531. 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

SNAP23. human.

EvolutionaryTrace

O00161.

GenomeRNAi

8773.

NextBio

32894.

PMAP-CutDB

O00161.

SOURCE

Search...

Entry information

Entry name

SNP23_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 139 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.