P17599 · SYN1_BOVIN

  • Protein
    Synapsin-1
  • Gene
    SYN1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    4/5

Function

function

Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal (By similarity).
Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity).
The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level (By similarity).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell projection
Cellular ComponentGolgi apparatus
Cellular Componentsynaptic vesicle
Cellular Componentsynaptic vesicle membrane
Molecular Functionactin binding
Molecular FunctionATP binding
Biological Processneurotransmitter secretion

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Synapsin-1
  • Alternative names
    • Synapsin I

Gene names

    • Name
      SYN1

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos

Accessions

  • Primary accession
    P17599

Proteomes

Subcellular Location

Synapse
Golgi apparatus
Presynapse
Note: Dissociates from synaptic vesicles and redistributes into the axon during action potential firing, in a step that precedes fusion of vesicles with the plasma membrane. Reclusters to presynapses after the cessation of synaptic activity.

Keywords

Phenotypes & Variants

PTM/Processing

Features

Showing features for chain, modified residue, glycosylation.

TypeIDPosition(s)Description
ChainPRO_00001830161-706Synapsin-1
Modified residue9Phosphoserine; by CaMK1 and PKA
Modified residue39Phosphoserine
Glycosylation55O-linked (GlcNAc) serine
Modified residue62Phosphoserine
Modified residue67Phosphoserine
Glycosylation87O-linked (GlcNAc) threonine
Glycosylation96O-linked (GlcNAc) serine
Glycosylation103O-linked (GlcNAc) serine
Glycosylation261O-linked (GlcNAc) serine
Modified residue312Phosphotyrosine
Modified residue427Phosphoserine
Modified residue430Omega-N-methylarginine
Modified residue432Phosphoserine; alternate
Glycosylation432O-linked (GlcNAc) serine; alternate
Modified residue434Phosphoserine
Modified residue436Phosphothreonine
Modified residue438Phosphoserine
Modified residue476Omega-N-methylarginine
Glycosylation526O-linked (GlcNAc) threonine
Modified residue534Omega-N-methylarginine
Modified residue547Omega-N-methylarginine
Modified residue551Phosphoserine; by PDPK1
Modified residue553Phosphoserine
Modified residue556Omega-N-methylarginine
Glycosylation564O-linked (GlcNAc) threonine
Modified residue568Phosphoserine; by CaMK2
Glycosylation578O-linked (GlcNAc) serine
Modified residue605Phosphoserine; by CaMK2
Modified residue622Omega-N-methylarginine
Modified residue664Phosphoserine
Modified residue666Phosphoserine
Modified residue680Asymmetric dimethylarginine
Modified residue684Phosphoserine

Post-translational modification

Substrate of different protein kinases. Phosphorylation, including phosphorylation at Ser-9, promotes synapsin-1 dissociation from synaptic vesicles, regulates its rate of dispersion, and controls the kinetics of vesicle pool turnover and neurotransmitter release (By similarity).

Keywords

Proteomic databases

PTM databases

Interaction

Subunit

Homodimer (By similarity).
Can form oligomers with SYN2 (By similarity).
Interacts with CAPON. Forms a ternary complex with NOS1 (By similarity).
Isoform Ib interacts with PRNP (By similarity).

Protein-protein interaction databases

Chemistry

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-23Polar residues
Region1-28A
Region1-72Disordered
Compositional bias25-41Pro residues
Region29-112B; linker
Region113-420C; actin-binding and synaptic-vesicle binding
Region418-690Disordered
Region421-656D; Pro-rich linker
Compositional bias428-445Polar residues
Compositional bias455-481Pro residues
Compositional bias513-533Polar residues
Compositional bias541-556Pro residues
Compositional bias557-574Polar residues
Compositional bias614-630Pro residues
Region657-706E

Domain

The A region binds phospholipids with a preference for negatively charged species.

Sequence similarities

Belongs to the synapsin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoform

Align isoforms (2)
  • Sequence status
    Complete

This entry describes 2 isoforms produced by Alternative splicing.

P17599-1

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.

  • Length
    706
  • Mass (Da)
    74,518
  • Last updated
    1996-02-01 v2
  • Checksum
    89373750BF014340
MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPAAPSPGATTGPATATAERASSAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSINSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLINQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATTEPFIDAKYDVRIQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIQVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPRQRQRDASPGRGSHSQTPSPGALPLGRQISQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPTPQGQQHLSGLGPPAGSPLPQRLPSPTSVPQQPASQATPMTQGQGRQSRPVAGGPGAPPATRPPASPSPQRQAGPPQATRQTSVSGQAPPKASGVPPGGQQRQGPPQKPPGPAGPTRQASQAGPMPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD

P17599-2

  • Name
    IB
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Features

Showing features for compositional bias, alternative sequence.

TypeIDPosition(s)Description
Compositional bias1-23Polar residues
Compositional bias25-41Pro residues
Compositional bias428-445Polar residues
Compositional bias455-481Pro residues
Compositional bias513-533Polar residues
Compositional bias541-556Pro residues
Compositional bias557-574Polar residues
Compositional bias614-630Pro residues
Alternative sequenceVSP_006314662-670in isoform IB
Alternative sequenceVSP_006315671-706in isoform IB

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M27810
EMBL· GenBank· DDBJ
AAA30761.1
EMBL· GenBank· DDBJ
mRNA
M27811
EMBL· GenBank· DDBJ
AAA30762.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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