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Protein

Synaptosomal-associated protein 29

Gene

SNAP29

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

Functioni

SNAREs, soluble N-ethylmaleimide-sensitive factor-attachment protein receptors, are essential proteins for fusion of cellular membranes. SNAREs localized on opposing membranes assemble to form a trans-SNARE complex, an extended, parallel four alpha-helical bundle that drives membrane fusion. SNAP29 is a SNARE involved in autophagy through the direct control of autophagosome membrane fusion with the lysososome membrane.2 Publications

GO - Molecular functioni

  • SNAP receptor activity Source: ProtInc
  • syntaxin binding Source: GO_Central

GO - Biological processi

  • autophagic vacuole fusion Source: UniProtKB
  • exocytosis Source: ProtInc
  • membrane fusion Source: ProtInc
  • protein transport Source: UniProtKB-KW
  • synaptic vesicle fusion to presynaptic membrane Source: GO_Central
  • synaptic vesicle priming Source: GO_Central
  • vesicle targeting Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Autophagy, Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Synaptosomal-associated protein 29Imported
Short name:
SNAP-29Imported
Alternative name(s):
Soluble 29 kDa NSF attachment proteinImported
Vesicle-membrane fusion protein SNAP-29
Gene namesi
Name:SNAP29Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11133. SNAP29.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • centrosome Source: HPA
  • cytoplasm Source: HPA
  • neuron projection Source: UniProtKB-SubCell
  • plasma membrane Source: ProtInc
  • SNARE complex Source: UniProtKB
  • synapse Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoplasmic vesicle, Golgi apparatus, Membrane

Pathology & Biotechi

Involvement in diseasei

Cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma syndrome (CEDNIK)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis and palmoplantar keratoderma.

See also OMIM:609528

Keywords - Diseasei

Ichthyosis, Neuropathy, Palmoplantar keratoderma

Organism-specific databases

MIMi609528. phenotype.
Orphaneti66631. CEDNIK syndrome.
PharmGKBiPA35981.

Polymorphism and mutation databases

BioMutaiSNAP29.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 258258Synaptosomal-associated protein 29PRO_0000213601Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95721.
PaxDbiO95721.
PeptideAtlasiO95721.
PRIDEiO95721.

PTM databases

PhosphoSiteiO95721.

Expressioni

Tissue specificityi

Found in brain, heart, kidney, liver, lung, placenta, skeletal muscle, spleen and pancreas.1 Publication

Gene expression databases

BgeeiO95721.
CleanExiHS_SNAP29.
ExpressionAtlasiO95721. baseline and differential.
GenevestigatoriO95721.

Organism-specific databases

HPAiCAB037092.
HPA031823.
HPA056492.

Interactioni

Subunit structurei

Forms a SNARE complex, composed of VAMP8, SNAP29 and STX17, involved in fusion of autophagosome with lysosome (PubMed:23217709, PubMed:25686604). Interacts with multiple syntaxins including STX6 (By similarity).By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FAM9BQ8IZU03EBI-490676,EBI-10175124
STX12Q86Y823EBI-490676,EBI-2691717
VAMP1P237633EBI-490676,EBI-10201335
VAMP2P630273EBI-490676,EBI-520113
VAMP4O75379-23EBI-490676,EBI-10187996
VAMP5O951833EBI-490676,EBI-10191195

Protein-protein interaction databases

BioGridi114748. 60 interactions.
DIPiDIP-56475N.
IntActiO95721. 21 interactions.
MINTiMINT-3003155.
STRINGi9606.ENSP00000215730.

Structurei

Secondary structure

1
258
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi40 – 11374Combined sources
Helixi195 – 25561Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WY4X-ray1.40C39-116[»]
D194-258[»]
ProteinModelPortaliO95721.
SMRiO95721. Positions 42-103, 197-255.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini196 – 25863t-SNARE coiled-coil homologyPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili76 – 10732Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the SNAP-25 family.Curated
Contains 1 t-SNARE coiled-coil homology domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG244202.
GeneTreeiENSGT00510000048053.
HOGENOMiHOG000046806.
HOVERGENiHBG057045.
InParanoidiO95721.
KOiK08509.
OMAiQEAQYQA.
OrthoDBiEOG7FNC8G.
PhylomeDBiO95721.
TreeFamiTF320226.

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. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAYPKSYNP FDDDGEDEGA RPAPWRDARD LPDGPDAPAD RQQYLRQEVL
60 70 80 90 100
RRAEATAAST SRSLALMYES EKVGVASSEE LARQRGVLER TEKMVDKMDQ
110 120 130 140 150
DLKISQKHIN SIKSVFGGLV NYFKSKPVET PPEQNGTLTS QPNNRLKEAI
160 170 180 190 200
STSKEQEAKY QASHPNLRKL DDTDPVPRGA GSAMSTDAYP KNPHLRAYHQ
210 220 230 240 250
KIDSNLDELS MGLGRLKDIA LGMQTEIEEQ DDILDRLTTK VDKLDVNIKS

TERKVRQL
Length:258
Mass (Da):28,970
Last modified:May 1, 1999 - v1
Checksum:i7E1CDBA22D6F5A3C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115436 mRNA. Translation: AAD11436.1.
AF278704 Genomic DNA. Translation: AAF91421.1.
CR456582 mRNA. Translation: CAG30468.1.
BT007357 mRNA. Translation: AAP36021.1.
BC009715 mRNA. Translation: AAH09715.1.
CCDSiCCDS13784.1.
RefSeqiNP_004773.1. NM_004782.3.
UniGeneiHs.108002.

Genome annotation databases

EnsembliENST00000215730; ENSP00000215730; ENSG00000099940.
GeneIDi9342.
KEGGihsa:9342.
UCSCiuc011ahw.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF115436 mRNA. Translation: AAD11436.1.
AF278704 Genomic DNA. Translation: AAF91421.1.
CR456582 mRNA. Translation: CAG30468.1.
BT007357 mRNA. Translation: AAP36021.1.
BC009715 mRNA. Translation: AAH09715.1.
CCDSiCCDS13784.1.
RefSeqiNP_004773.1. NM_004782.3.
UniGeneiHs.108002.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WY4X-ray1.40C39-116[»]
D194-258[»]
ProteinModelPortaliO95721.
SMRiO95721. Positions 42-103, 197-255.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114748. 60 interactions.
DIPiDIP-56475N.
IntActiO95721. 21 interactions.
MINTiMINT-3003155.
STRINGi9606.ENSP00000215730.

PTM databases

PhosphoSiteiO95721.

Polymorphism and mutation databases

BioMutaiSNAP29.

Proteomic databases

MaxQBiO95721.
PaxDbiO95721.
PeptideAtlasiO95721.
PRIDEiO95721.

Protocols and materials databases

DNASUi9342.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000215730; ENSP00000215730; ENSG00000099940.
GeneIDi9342.
KEGGihsa:9342.
UCSCiuc011ahw.2. human.

Organism-specific databases

CTDi9342.
GeneCardsiGC22P021213.
HGNCiHGNC:11133. SNAP29.
HPAiCAB037092.
HPA031823.
HPA056492.
MIMi604202. gene.
609528. phenotype.
neXtProtiNX_O95721.
Orphaneti66631. CEDNIK syndrome.
PharmGKBiPA35981.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244202.
GeneTreeiENSGT00510000048053.
HOGENOMiHOG000046806.
HOVERGENiHBG057045.
InParanoidiO95721.
KOiK08509.
OMAiQEAQYQA.
OrthoDBiEOG7FNC8G.
PhylomeDBiO95721.
TreeFamiTF320226.

Miscellaneous databases

ChiTaRSiSNAP29. human.
GeneWikiiSNAP29.
GenomeRNAii9342.
NextBioi34991.
PROiO95721.
SOURCEiSearch...

Gene expression databases

BgeeiO95721.
CleanExiHS_SNAP29.
ExpressionAtlasiO95721. baseline and differential.
GenevestigatoriO95721.

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. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Brain.
  2. "Genomic organization of the human SNAP29 gene."
    Schardt A., Kraemer E.-M., Werner H., Nave K.-A.
    Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
  5. "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].
    Tissue: Pancreas.
  6. "A mutation in SNAP29, coding for a SNARE protein involved in intracellular trafficking, causes a novel neurocutaneous syndrome characterized by cerebral dysgenesis, neuropathy, ichthyosis, and palmoplantar keratoderma."
    Sprecher E., Ishida-Yamamoto A., Mizrahi-Koren M., Rapaport D., Goldsher D., Indelman M., Topaz O., Chefetz I., Keren H., O'brien T.J., Bercovich D., Shalev S., Geiger D., Bergman R., Horowitz M., Mandel H.
    Am. J. Hum. Genet. 77:242-251(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN CEDNIK.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes."
    Itakura E., Kishi-Itakura C., Mizushima N.
    Cell 151:1256-1269(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AUTOPHAGY, INTERACTION WITH VAMP8 AND STX17.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. "ATG14 promotes membrane tethering and fusion of autophagosomes to endolysosomes."
    Diao J., Liu R., Rong Y., Zhao M., Zhang J., Lai Y., Zhou Q., Wilz L.M., Li J., Vivona S., Pfuetzner R.A., Brunger A.T., Zhong Q.
    Nature 0:0-0(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 39-116 AND 194-258 IN COMPLEX WITH STX17 AND VAMP8, SUBCELLULAR LOCATION, FUNCTION.

Entry informationi

Entry nameiSNP29_HUMAN
AccessioniPrimary (citable) accession number: O95721
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 27, 2015
This is version 140 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, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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.