P17599 · SYN1_BOVIN
- ProteinSynapsin-1
- GeneSYN1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids706 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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 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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Aspect | Term | |
---|---|---|
Cellular Component | cell projection | |
Cellular Component | Golgi apparatus | |
Cellular Component | synaptic vesicle | |
Cellular Component | synaptic vesicle membrane | |
Molecular Function | actin binding | |
Molecular Function | ATP binding | |
Biological Process | neurotransmitter secretion |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameSynapsin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP17599
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
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
- Cellular component
Phenotypes & Variants
Chemistry
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000183016 | 1-706 | Synapsin-1 | |||
Sequence: MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPAAPSPGATTGPATATAERASSAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSINSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLINQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATTEPFIDAKYDVRIQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIQVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPRQRQRDASPGRGSHSQTPSPGALPLGRQISQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPTPQGQQHLSGLGPPAGSPLPQRLPSPTSVPQQPASQATPMTQGQGRQSRPVAGGPGAPPATRPPASPSPQRQAGPPQATRQTSVSGQAPPKASGVPPGGQQRQGPPQKPPGPAGPTRQASQAGPMPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD | ||||||
Modified residue | 9 | Phosphoserine; by CaMK1 and PKA | ||||
Sequence: S | ||||||
Modified residue | 39 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 55 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 62 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 67 | Phosphoserine | ||||
Sequence: S | ||||||
Glycosylation | 87 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Glycosylation | 96 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Glycosylation | 103 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Glycosylation | 261 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 312 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 427 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 430 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 432 | Phosphoserine; alternate | ||||
Sequence: S | ||||||
Glycosylation | 432 | O-linked (GlcNAc) serine; alternate | ||||
Sequence: S | ||||||
Modified residue | 434 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 436 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 438 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 476 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Glycosylation | 526 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 534 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 547 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 551 | Phosphoserine; by PDPK1 | ||||
Sequence: S | ||||||
Modified residue | 553 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 556 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Glycosylation | 564 | O-linked (GlcNAc) threonine | ||||
Sequence: T | ||||||
Modified residue | 568 | Phosphoserine; by CaMK2 | ||||
Sequence: S | ||||||
Glycosylation | 578 | O-linked (GlcNAc) serine | ||||
Sequence: S | ||||||
Modified residue | 605 | Phosphoserine; by CaMK2 | ||||
Sequence: S | ||||||
Modified residue | 622 | Omega-N-methylarginine | ||||
Sequence: R | ||||||
Modified residue | 664 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 666 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 680 | Asymmetric dimethylarginine | ||||
Sequence: R | ||||||
Modified residue | 684 | Phosphoserine | ||||
Sequence: S |
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
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Polar residues | ||||
Sequence: MNYLRRRLSDSNFMANLPNGYMT | ||||||
Region | 1-28 | A | ||||
Sequence: MNYLRRRLSDSNFMANLPNGYMTDLQRP | ||||||
Region | 1-72 | Disordered | ||||
Sequence: MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPAAPSPGATTGPATATAERASSAAPVASPAAPSPGSSG | ||||||
Compositional bias | 25-41 | Pro residues | ||||
Sequence: LQRPQPPPPPPAAPSPG | ||||||
Region | 29-112 | B; linker | ||||
Sequence: QPPPPPPAAPSPGATTGPATATAERASSAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAA | ||||||
Region | 113-420 | C; actin-binding and synaptic-vesicle binding | ||||
Sequence: ARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSINSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLINQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATTEPFIDAKYDVRIQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIQVVGSSMPLIGDHQDEDKQLIVELVVNKMAQALPR | ||||||
Region | 418-690 | Disordered | ||||
Sequence: LPRQRQRDASPGRGSHSQTPSPGALPLGRQISQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPTPQGQQHLSGLGPPAGSPLPQRLPSPTSVPQQPASQATPMTQGQGRQSRPVAGGPGAPPATRPPASPSPQRQAGPPQATRQTSVSGQAPPKASGVPPGGQQRQGPPQKPPGPAGPTRQASQAGPMPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPATAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKA | ||||||
Region | 421-656 | D; Pro-rich linker | ||||
Sequence: QRQRDASPGRGSHSQTPSPGALPLGRQISQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPTPQGQQHLSGLGPPAGSPLPQRLPSPTSVPQQPASQATPMTQGQGRQSRPVAGGPGAPPATRPPASPSPQRQAGPPQATRQTSVSGQAPPKASGVPPGGQQRQGPPQKPPGPAGPTRQASQAGPMPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPATAAAGGP | ||||||
Compositional bias | 428-445 | Polar residues | ||||
Sequence: PGRGSHSQTPSPGALPLG | ||||||
Compositional bias | 455-481 | Pro residues | ||||
Sequence: PPAQQRPPPQGGPPQPGPGPQRQGPPL | ||||||
Compositional bias | 513-533 | Polar residues | ||||
Sequence: SVPQQPASQATPMTQGQGRQS | ||||||
Compositional bias | 541-556 | Pro residues | ||||
Sequence: GAPPATRPPASPSPQR | ||||||
Compositional bias | 557-574 | Polar residues | ||||
Sequence: QAGPPQATRQTSVSGQAP | ||||||
Compositional bias | 614-630 | Pro residues | ||||
Sequence: GPPTTQQPRPSGPGPAG | ||||||
Region | 657-706 | E | ||||
Sequence: PHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD |
Domain
The A region binds phospholipids with a preference for negatively charged species.
Sequence similarities
Belongs to the synapsin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
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.
- NameIA
- Length706
- Mass (Da)74,518
- Last updated1996-02-01 v2
- Checksum89373750BF014340
P17599-2
- NameIB
Features
Showing features for compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-23 | Polar residues | ||||
Sequence: MNYLRRRLSDSNFMANLPNGYMT | ||||||
Compositional bias | 25-41 | Pro residues | ||||
Sequence: LQRPQPPPPPPAAPSPG | ||||||
Compositional bias | 428-445 | Polar residues | ||||
Sequence: PGRGSHSQTPSPGALPLG | ||||||
Compositional bias | 455-481 | Pro residues | ||||
Sequence: PPAQQRPPPQGGPPQPGPGPQRQGPPL | ||||||
Compositional bias | 513-533 | Polar residues | ||||
Sequence: SVPQQPASQATPMTQGQGRQS | ||||||
Compositional bias | 541-556 | Pro residues | ||||
Sequence: GAPPATRPPASPSPQR | ||||||
Compositional bias | 557-574 | Polar residues | ||||
Sequence: QAGPPQATRQTSVSGQAP | ||||||
Compositional bias | 614-630 | Pro residues | ||||
Sequence: GPPTTQQPRPSGPGPAG | ||||||
Alternative sequence | VSP_006314 | 662-670 | in isoform IB | |||
Sequence: NKSQSLTNA → KASPAQAQP | ||||||
Alternative sequence | VSP_006315 | 671-706 | in isoform IB | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
M27810 EMBL· GenBank· DDBJ | AAA30761.1 EMBL· GenBank· DDBJ | mRNA | ||
M27811 EMBL· GenBank· DDBJ | AAA30762.1 EMBL· GenBank· DDBJ | mRNA |