O00161 · SNP23_HUMAN
- ProteinSynaptosomal-associated protein 23
- GeneSNAP23
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids211 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Essential component of the high affinity receptor for the general membrane fusion machinery and an important regulator of transport vesicle docking and fusion.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameSynaptosomal-associated protein 23
- Short namesSNAP-23
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO00161
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cell membrane ; Peripheral membrane protein
Cell membrane ; Lipid-anchor
Note: Mainly localized to the plasma membrane.
Keywords
- Cellular component
Disease & Variants
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 179 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue, chain, modified residue (large scale data), lipidation.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue | 1 | UniProt | N-acetylmethionine | ||||
Sequence: M | |||||||
Chain | PRO_0000213598 | 1-211 | UniProt | Synaptosomal-associated protein 23 | |||
Sequence: MDNLSSEEIQQRAHQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTELNKCCGLCVCPCNRTKNFESGKAYKTTWGDGGENSPCNVVSKQPGPVTNGQLQQPTTGAASGGYIKRITNDAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKLIDS | |||||||
Modified residue | 5 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 5 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 6 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 6 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 20 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 20 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 23 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 34 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 34 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 41 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 43 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Lipidation | 79 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 80 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 83 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 85 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Lipidation | 87 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 101 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 110 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 110 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Lipidation | 112 | UniProt | S-palmitoyl cysteine | ||||
Sequence: C | |||||||
Modified residue (large scale data) | 136 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 139 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 144 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 157 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 161 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 161 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
2D gel databases
PTM databases
Expression
Tissue specificity
Ubiquitous. Highest levels where found in placenta.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Homotetramer (via coiled-coil domain), also forms heterotetramers with STX4 and VAMP3 (PubMed:12556468).
Found in a complex with VAMP8 and STX1A (PubMed:12130530).
Found in a complex with VAMP8 and STX4 in pancreas (By similarity).
Interacts simultaneously with SNAPIN and SYN4 (By similarity).
Interacts with STX1A (By similarity).
Interacts with STX12 (By similarity).
Interacts tightly to multiple syntaxins and synaptobrevins/VAMPs (By similarity).
Interacts with ZDHHC13 (via ANK repeats) (By similarity).
Interacts with ZDHHC17 (via ANK repeats) (PubMed:28882895).
Found in a complex with VAMP8 and STX1A (PubMed:12130530).
Found in a complex with VAMP8 and STX4 in pancreas (By similarity).
Interacts simultaneously with SNAPIN and SYN4 (By similarity).
Interacts with STX1A (By similarity).
Interacts with STX12 (By similarity).
Interacts tightly to multiple syntaxins and synaptobrevins/VAMPs (By similarity).
Interacts with ZDHHC13 (via ANK repeats) (By similarity).
Interacts with ZDHHC17 (via ANK repeats) (PubMed:28882895).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O00161 | NAPA P54920 | 5 | EBI-745000, EBI-749652 | |
BINARY | O00161 | NAPB Q9H115 | 3 | EBI-745000, EBI-3921185 | |
BINARY | O00161 | SCGN O76038 | 3 | EBI-745000, EBI-749420 | |
BINARY | O00161 | STX11 O75558 | 11 | EBI-745000, EBI-714135 | |
BINARY | O00161 | VAMP3 Q15836 | 3 | EBI-745000, EBI-722343 | |
BINARY | O00161 | ZDHHC17 Q8IUH5 | 4 | EBI-745000, EBI-524753 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-20 | Disordered | ||||
Sequence: MDNLSSEEIQQRAHQITDES | ||||||
Domain | 14-76 | t-SNARE coiled-coil homology 1 | ||||
Sequence: HQITDESLESTRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTEL | ||||||
Coiled coil | 23-76 | |||||
Sequence: STRRILGLAIESQDAGIKTITMLDEQKEQLNRIEEGLDQINKDMRETEKTLTEL | ||||||
Domain | 146-208 | t-SNARE coiled-coil homology 2 | ||||
Sequence: DAREDEMEENLTQVGSILGNLKDMALNIGNEIDAQNPQIKRITDKADTNRDRIDIANARAKKL |
Sequence similarities
Belongs to the SNAP-25 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
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.
- NameSNAP-23a
- Length211
- Mass (Da)23,354
- Last updated1997-07-01 v1
- ChecksumAC378E9786C3A239
O00161-2
- NameSNAP-23b
Computationally mapped potential isoform sequences
There are 10 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U55936 EMBL· GenBank· DDBJ | AAC50537.1 EMBL· GenBank· DDBJ | mRNA | ||
Y09567 EMBL· GenBank· DDBJ | CAA70760.1 EMBL· GenBank· DDBJ | mRNA | ||
Y09568 EMBL· GenBank· DDBJ | CAA70761.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ011915 EMBL· GenBank· DDBJ | CAA09864.1 EMBL· GenBank· DDBJ | mRNA | ||
AJ278972 EMBL· GenBank· DDBJ | CAC07504.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ278973 EMBL· GenBank· DDBJ | CAC07504.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AJ278974 EMBL· GenBank· DDBJ | CAC07504.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BT006916 EMBL· GenBank· DDBJ | AAP35562.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457212 EMBL· GenBank· DDBJ | CAG33493.1 EMBL· GenBank· DDBJ | mRNA | ||
BC000148 EMBL· GenBank· DDBJ | AAH00148.1 EMBL· GenBank· DDBJ | mRNA | ||
BC003686 EMBL· GenBank· DDBJ | AAH03686.1 EMBL· GenBank· DDBJ | mRNA | ||
BC022890 EMBL· GenBank· DDBJ | AAH22890.1 EMBL· GenBank· DDBJ | mRNA |