O88935 (SYN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 116.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Synapsin-1 Alternative name(s): Synapsin I | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus![]() |
Protein attributes
| Sequence length | 706 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release. Regulation of neurotransmitter release. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxide functions at a presynaptic level. |
| Subunit structure | Homodimer. Interacts with CAPON. Forms a ternary complex with NOS1 By similarity. Isoform Ib interacts with PRNP. Ref.5 |
| Subcellular location | |
| Domain | The A region binds phospholipids with a preference for negatively charged species By similarity. |
| Post-translational modification | Substrate of at least four different protein kinases. It is probable that phosphorylation plays a role in the regulation of synapsin-1 in the nerve terminal By similarity. Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles By similarity. |
| Sequence similarities | Belongs to the synapsin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Golgi apparatus Synapse |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Ligand | Actin-binding |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | metabolic process Inferred from electronic annotation. Source: GOC neurotransmitter secretionInferred from electronic annotation. Source: InterPro |
| Cellular_component | Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell junctionInferred from electronic annotation. Source: UniProtKB-KW cytosolInferred from electronic annotation. Source: Compara dendriteInferred from electronic annotation. Source: Compara synaptic vesicleInferred from electronic annotation. Source: Compara |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: InterPro catalytic activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Ia (identifier: O88935-2) 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 Ib (identifier: O88935-1) The sequence of this isoform differs from the canonical sequence as follows: 662-670: NKSQSLTNA → KASPSQAQP 671-706: Missing. | ||||||
| Isoform 3 (identifier: O88935-3) The sequence of this isoform differs from the canonical sequence as follows: 573-600: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 706 | 706 | Synapsin-1 | PRO_0000183019 | |||||
Regions | |||||||||
| Region | 1 – 28 | 28 | A | ||||||
| Region | 29 – 112 | 84 | B; linker | ||||||
| Region | 113 – 420 | 308 | C; actin-binding and synaptic-vesicle binding | ||||||
| Region | 421 – 657 | 237 | D; Pro-rich linker | ||||||
| Region | 658 – 706 | 49 | E | ||||||
Amino acid modifications | |||||||||
| Modified residue | 9 | 1 | Phosphoserine; by CaMK1 and PKA; alternate By similarity | ||||||
| Modified residue | 9 | 1 | Phosphoserine; by PKA and CaMK1; alternate By similarity | ||||||
| Modified residue | 62 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 67 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 312 | 1 | Phosphotyrosine Ref.9 | ||||||
| Modified residue | 337 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 427 | 1 | Phosphoserine Ref.7 Ref.10 | ||||||
| Modified residue | 510 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 512 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 520 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 551 | 1 | Phosphoserine; by PDPK1 By similarity | ||||||
| Modified residue | 553 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 568 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 605 | 1 | Phosphoserine; by CaMK2 By similarity | ||||||
| Modified residue | 666 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 705 | 1 | Phosphoserine Ref.10 | ||||||
| Glycosylation | 55 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 56 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 87 | 1 | O-linked (GlcNAc) Ref.8 | ||||||
| Glycosylation | 96 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 103 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 261 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 432 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 518 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 526 | 1 | O-linked (GlcNAc) Ref.8 | ||||||
| Glycosylation | 564 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 578 | 1 | O-linked (GlcNAc) By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 573 – 600 | 28 | Missing in isoform 3. | VSP_015205 | |||||
| Alternative sequence | 662 – 670 | 9 | NKSQSLTNA → KASPSQAQP in isoform Ib. | VSP_015206 | |||||
| Alternative sequence | 671 – 706 | 36 | Missing in isoform Ib. | VSP_015207 | |||||
Experimental info | |||||||||
| Sequence conflict | 44 | 1 | P → L in AAA79963. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Cloning from insulinoma cells of synapsin I associated with insulin secretory granules." Matsumoto K., Ebihara K., Yamamoto H., Tabuchi H., Fukunaga K., Yasunami M., Ohkubo H., Shichiri M., Miyamoto E. J. Biol. Chem. 274:2053-2059(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IB). Strain: C57BL/6. Tissue: Pancreatic islet. |
| [2] | "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 3). Tissue: Eye. |
| [3] | "Neuron-specific expression of the synapsin II gene is directed by a specific core promoter and upstream regulatory elements." Chin L.S., Li L., Greengard P. J. Biol. Chem. 269:18507-18513(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. |
| [4] | Lubec G., Kang S.U., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 86-108; 115-128; 177-186; 257-269; 282-311; 329-336; 414-420; 431-446 AND 566-576, MASS SPECTROMETRY. Strain: C57BL/6 and OF1. Tissue: Brain and Hippocampus. |
| [5] | "PrPC directly interacts with proteins involved in signaling pathways." Spielhaupter C., Schaetzl H.M. J. Biol. Chem. 276:44604-44612(2001) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PRNP. |
| [6] | "Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-510, MASS SPECTROMETRY. Tissue: Embryonic brain. |
| [7] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427 AND SER-568, MASS SPECTROMETRY. Tissue: Brain. |
| [8] | "O-linked N-acetylglucosamine proteomics of postsynaptic density preparations using lectin weak affinity chromatography and mass spectrometry." Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A., Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:923-934(2006) [PubMed] [Europe PMC] [Abstract] Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-87 AND THR-526, MASS SPECTROMETRY. Tissue: Brain. |
| [9] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, MASS SPECTROMETRY. Tissue: Brain. |
| [10] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62; SER-67; THR-337; SER-427; THR-512; SER-520; SER-553; SER-666 AND SER-705, MASS SPECTROMETRY. Tissue: Brain cortex. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AF085809 mRNA. Translation: AAD09833.1. BC022954 mRNA. Translation: AAH22954.1. L32025 Genomic DNA. Translation: AAA79963.1. |
| IPI | IPI00136372. IPI00649467. IPI00649886. |
| PIR | A53692. |
| RefSeq | NP_001104250.1. NM_001110780.1. NP_038708.3. NM_013680.4. |
| UniGene | Mm.439844. |
3D structure databases | |
| ProteinModelPortal | O88935. |
| SMR | O88935. Positions 112-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O88935. 10 interactions. |
| MINT | MINT-1531899. |
PTM databases | |
| PhosphoSite | O88935. |
Proteomic databases | |
| PaxDb | O88935. |
| PRIDE | O88935. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000081893; ENSMUSP00000080568; ENSMUSG00000037217. ENSMUST00000115345; ENSMUSP00000111002; ENSMUSG00000037217. |
| GeneID | 20964. |
| KEGG | mmu:20964. |
| UCSC | uc009stw.2. mouse. |
Organism-specific databases | |
| CTD | 6853. |
| MGI | MGI:98460. Syn1. |
Phylogenomic databases | |
| eggNOG | NOG284201. |
| GeneTree | ENSGT00530000063319. |
| HOGENOM | HOG000231323. |
| HOVERGEN | HBG016354. |
| InParanoid | O88935. |
Gene expression databases | |
| ArrayExpress | O88935. |
| Bgee | O88935. |
| CleanEx | MM_SYN1. |
| Genevestigator | O88935. |
| GermOnline | ENSMUSG00000037217. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.30.1490.20. 1 hit. 3.30.470.20. 2 hits. 3.40.50.20. 1 hit. |
| InterPro | IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR016185. PreATP-grasp_dom. IPR001359. Synapsin. IPR020898. Synapsin_ATP-bd_dom. IPR019735. Synapsin_CS. IPR019736. Synapsin_P_site. IPR020897. Synapsin_pre-ATP-grasp_dom. [Graphical view] |
| Pfam | PF02078. Synapsin. 1 hit. PF02750. Synapsin_C. 1 hit. PF10581. Synapsin_N. 1 hit. [Graphical view] |
| PRINTS | PR01368. SYNAPSIN. |
| SUPFAM | SSF52440. PreATP-grasp-like. 1 hit. |
| PROSITE | PS00415. SYNAPSIN_1. 1 hit. PS00416. SYNAPSIN_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 299922. |
| SOURCE | Search... |
Entry information
| Entry name | SYN1_MOUSE | ||||||||
| Accession | Primary (citable) accession number: O88935 Secondary accession number(s): Q62279, Q8QZT8 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
