O88778 (BSN_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 79.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Protein bassoon | ||
| Gene names |
| ||
| Organism | Rattus norvegicus (Rat) | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 3938 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Is thought to be involved in the organization of the cytomatrix at the nerve terminals active zone (CAZ) which regulates neurotransmitter release. Seems to act through binding to ERC2/CAST1. Essential in regulated neurotransmitter release from a subset of brain glutamatergic synapses. Involved in the formation of the retinal photoreceptor ribbon synapses By similarity. Ref.5 |
| Subunit structure | Interacts with ERC2/CAST1, RIMS1 and UNC13A. Part of a complex consisting of ERC2, RIMS1 and BSN. Ref.4 Ref.5 |
| Subcellular location | Cytoplasm. Cell junction › synapse › synaptosome. Cytoplasm › cytoskeleton. Note: Localized to the active zone of presynaptic density. In retina, is localized in the outer plexiform layer at ribbon synapses formed by rods and cones but was absent from basal synaptic contacts formed by cones. In the retinal inner plexiform layer localized to conventional inhibitory GABAergic synapses, made by amacrine cells, but absent from the bipolar cell ribbon synapses. Ref.1 Ref.2 Ref.3 |
| Developmental stage | Detected at embryonic day E18 and at later stages. The expression does not significantly change during the developmental stages tested. Ref.4 |
| Post-translational modification | Myristoylated. The N-terminal myristoylation is not sufficient for presynaptic localization. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Cytoplasm Cytoskeleton Synapse Synaptosome |
| Domain | Coiled coil Repeat Zinc-finger |
| Ligand | Metal-binding Zinc |
| PTM | Glycoprotein Lipoprotein Myristate Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | cytoskeleton organization Non-traceable author statement Ref.1. Source: RGD |
| Cellular component | cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytoplasmInferred from electronic annotation. Source: UniProtKB-SubCell cytoskeletonInferred from electronic annotation. Source: UniProtKB-SubCell excitatory synapseInferred from direct assay. Source: BHF-UCL synaptosomeInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction Ref.4. Source: RGD |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed | ||||||
| Chain | 2 – 3938 | 3937 | Protein bassoon | PRO_0000065004 | |||||
Regions | |||||||||
| Repeat | 568 – 574 | 7 | 1 | ||||||
| Repeat | 575 – 581 | 7 | 2 | ||||||
| Repeat | 582 – 588 | 7 | 3 | ||||||
| Zinc finger | 167 – 190 | 24 | C4-type Potential | ||||||
| Zinc finger | 195 – 217 | 23 | C4-type Potential | ||||||
| Zinc finger | 462 – 485 | 24 | C4-type Potential | ||||||
| Zinc finger | 490 – 512 | 23 | C4-type Potential | ||||||
| Region | 62 – 70 | 9 | 4 X 2 AA tandem repeats of P-G | ||||||
| Region | 568 – 588 | 21 | 3 X 7 AA tandem repeats of K-A-S-P-Q-A-[AK] | ||||||
| Region | 2934 – 2996 | 63 | Sufficient for binding to ERC2 | ||||||
| Coiled coil | 1032 – 1087 | 56 | Potential | ||||||
| Coiled coil | 1176 – 1203 | 28 | Potential | ||||||
| Coiled coil | 2345 – 2470 | 126 | Potential | ||||||
| Coiled coil | 2933 – 2975 | 43 | Potential | ||||||
| Coiled coil | 3772 – 3803 | 32 | Potential | ||||||
| Compositional bias | 2594 – 2600 | 7 | Poly-Arg | ||||||
| Compositional bias | 2621 – 2626 | 6 | Poly-Arg | ||||||
| Compositional bias | 2647 – 2654 | 8 | Poly-Ala | ||||||
| Compositional bias | 3770 – 3797 | 28 | Poly-Gln | ||||||
Amino acid modifications | |||||||||
| Modified residue | 6 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 105 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 135 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 140 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 142 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 965 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1004 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1087 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1090 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1093 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1099 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1101 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1121 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1221 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1469 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1470 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1474 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1481 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1483 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1485 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1498 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1541 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1542 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2017 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2032 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 2061 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 2112 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2564 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2581 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2608 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2679 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2688 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2793 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2796 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2807 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2843 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2845 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2851 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2893 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3007 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3286 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3368 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 3417 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 3418 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 3445 | 1 | Phosphotyrosine By similarity | ||||||
| Lipidation | 2 | 1 | N-myristoyl glycine Ref.3 | ||||||
| Glycosylation | 1339 | 1 | O-linked (GlcNAc) Ref.6 | ||||||
| Glycosylation | 1380 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 1922 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 2307 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 2510 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 2685 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 2930 | 1 | O-linked (GlcNAc) By similarity | ||||||
Experimental info | |||||||||
| Mutagenesis | 2 | 1 | G → A: Loss of myristoylation. Ref.3 | ||||||
Sequences
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References
| [1] | "Bassoon, a novel zinc-finger CAG/Glutamine-repeat protein selectively localized at the active zone of presynaptic nerve terminals." tom Dieck S., Sanmarti-Vila L., Langnaese K., Richter K., Kindler S., Soyke A., Wex H., Smalla K.-H., Kaempf U., Fraenzer J.-T., Stumm M., Garner C.C., Gundelfinger E.D. J. Cell Biol. 142:499-509(1998) [PubMed: 9679147] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION. Strain: Sprague-Dawley. Tissue: Brain. |
| [2] | "Differential expression of the presynaptic cytomatrix protein bassoon among ribbon synapses in the mammalian retina." Brandstatter J.H., Fletcher E.L., Garner C.C., Gundelfinger E.D., Wassle H. Eur. J. Neurosci. 11:3683-3693(1999) [PubMed: 10564375] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [3] | "Functional regions of the presynaptic cytomatrix protein bassoon: significance for synaptic targeting and cytomatrix anchoring." Dresbach T., Hempelmann A., Spilker C., tom Dieck S., Altrock W.D., Zuschratter W., Garner C.C., Gundelfinger E.D. Mol. Cell. Neurosci. 23:279-291(2003) [PubMed: 12812759] [Abstract] Cited for: SUBCELLULAR LOCATION, MYRISTOYLATION AT GLY-2, MUTAGENESIS OF GLY-2. |
| [4] | "Cast: a novel protein of the cytomatrix at the active zone of synapses that forms a ternary complex with RIM1 and Munc13-1." Ohtsuka T., Takao-Rikitsu E., Inoue E., Inoue M., Takeuchi M., Matsubara K., Deguchi-Tawarada M., Satoh K., Morimoto K., Nakanishi H., Takai Y. J. Cell Biol. 158:577-590(2002) [PubMed: 12163476] [Abstract] Cited for: INTERACTION WITH ERC2; RIMS1 AND UNC13A, DEVELOPMENTAL STAGE. |
| [5] | "Physical and functional interaction of the active zone proteins, CAST, RIM1, and Bassoon, in neurotransmitter release." Takao-Rikitsu E., Mochida S., Inoue E., Deguchi-Tawarada M., Inoue M., Ohtsuka T., Takai Y. J. Cell Biol. 164:301-311(2004) [PubMed: 14734538] [Abstract] Cited for: FUNCTION, INTERACTION WITH ERC2; RIMS1 AND UNC13A, IDENTIFICATION IN A COMPLEX WITH RIMS1 AND ERC2. |
| [6] | "Exploring the O-GlcNAc proteome: direct identification of O-GlcNAc-modified proteins from the brain." Khidekel N., Ficarro S.B., Peters E.C., Hsieh-Wilson L.C. Proc. Natl. Acad. Sci. U.S.A. 101:13132-13137(2004) [PubMed: 15340146] [Abstract] Cited for: GLYCOSYLATION AT THR-1339. Tissue: Brain. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | Y16563 mRNA. Translation: CAA76287.1. |
| IPI | IPI00212553. |
| PIR | T42761. |
| UniGene | Rn.29999. |
3D structure databases | |
| ProteinModelPortal | O88778. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O88778. 1 interaction. |
| MINT | MINT-4508415. |
| STRING | O88778. |
PTM databases | |
| PhosphoSite | O88778. |
Proteomic databases | |
| PRIDE | O88778. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Organism-specific databases | |
| RGD | 2223. Bsn. |
Phylogenomic databases | |
| eggNOG | roNOG04262. |
| GeneTree | ENSGT00600000084529. |
| HOVERGEN | HBG080934. |
| InParanoid | O88778. |
| OrthoDB | EOG4G4GPH. |
Gene expression databases | |
| ArrayExpress | O88778. |
| Genevestigator | O88778. |
| GermOnline | ENSRNOG00000030714. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR011011. Znf_FYVE_PHD. IPR008899. Znf_piccolo. IPR013083. Znf_RING/FYVE/PHD. [Graphical view] |
| Gene3D | G3DSA:3.30.40.10. Znf_RING/FYVE/PHD. 2 hits. |
| Pfam | PF05715. zf-piccolo. 2 hits. [Graphical view] |
| SUPFAM | SSF57903. FYVE_PHD_ZnF. 2 hits. |
| ProtoNet | Search... |
Entry information
| Entry name | BSN_RAT | ||||||||
| Accession | Primary (citable) accession number: O88778 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||

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