P17600 (SYN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 123.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Synapsin-1 Alternative name(s): Brain protein 4.1 Synapsin I | ||
| Gene names |
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| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 705 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. The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxid functions at a presynaptic level. |
| Subunit structure | Homodimer. Interacts with CAPON. Forms a ternary complex with NOS1. Isoform Ib interacts with PRNP By similarity. |
| Subcellular location | Cell junction › synapse. Golgi apparatus 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. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 |
| Involvement in disease | Defects in SYN1 are a cause of epilepsy X-linked with variable learning disabilities and behavior disorders (XELBD) [MIM:300491]. XELBD is characterized by variable combinations of epilepsy, learning difficulties, macrocephaly, and aggressive behavior. Ref.5 |
| Sequence similarities | Belongs to the synapsin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cell junction Golgi apparatus Synapse |
| Coding sequence diversity | Alternative splicing |
| Disease | Epilepsy |
| Domain | Repeat |
| Ligand | Actin-binding |
| PTM | Glycoprotein Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular component | Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cell junctionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: InterPro actin bindingInferred from electronic annotation. Source: UniProtKB-KW ligase activityInferred from electronic annotation. Source: InterPro transporter activityTraceable author statement. Source: ProtInc |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform IA (identifier: P17600-1) 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. | ||||||
| Isoform IB (identifier: P17600-2) The sequence of this isoform differs from the canonical sequence as follows: 661-669: NKSQSLTNA → KASPAQAQP 670-705: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 705 | 705 | Synapsin-1 | PRO_0000183018 | |||||
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 – 655 | 235 | D; Pro-rich linker | ||||||
| Region | 656 – 705 | 50 | E | ||||||
Amino acid modifications | |||||||||
| Modified residue | 9 | 1 | Phosphoserine; by CaMK1 and PKA | ||||||
| Modified residue | 39 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 62 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 67 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 312 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 337 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 427 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 510 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 512 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 520 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 551 | 1 | Phosphoserine; by PDPK1 Ref.6 | ||||||
| Modified residue | 553 | 1 | Phosphoserine Ref.6 | ||||||
| Modified residue | 568 | 1 | Phosphoserine; by CaMK2 | ||||||
| Modified residue | 605 | 1 | Phosphoserine; by CaMK2 Ref.6 Ref.7 | ||||||
| Modified residue | 665 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 704 | 1 | Phosphoserine By similarity | ||||||
| Glycosylation | 55 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 87 | 1 | O-linked (GlcNAc) By similarity | ||||||
| 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 | 526 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 564 | 1 | O-linked (GlcNAc) By similarity | ||||||
| Glycosylation | 578 | 1 | O-linked (GlcNAc) By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 661 – 669 | 9 | NKSQSLTNA → KASPAQAQP in isoform IB. | VSP_006316 | |||||
| Alternative sequence | 670 – 705 | 36 | Missing in isoform IB. | VSP_006317 | |||||
Experimental info | |||||||||
| Sequence conflict | 138 | 1 | E → G in AAC41930. Ref.1 | ||||||
| Sequence conflict | 138 | 1 | E → G in AAC41931. Ref.1 | ||||||
| Sequence conflict | 631 | 1 | R → A in AAC41930. Ref.1 | ||||||
| Sequence conflict | 631 | 1 | R → A in AAC41931. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The structure of the human synapsin I gene and protein." Suedhof T.C. J. Biol. Chem. 265:7849-7852(1990) [PubMed: 2110562] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING. Tissue: Brain. |
| [2] | "The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. Bentley D.R.Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "The 5'-flanking region of the synapsin I gene. A G+C-rich, TATA- and CAAT-less, phylogenetically conserved sequence with cell type-specific promoter function." Sauerwald A., Hoesche C., Oschwald R., Kilimann M.W. J. Biol. Chem. 265:14932-14937(1990) [PubMed: 2118519] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125. |
| [5] | "Identification of a mutation in synapsin I, a synaptic vesicle protein, in a family with epilepsy." Garcia C.C., Blair H.J., Seager M., Coulthard A., Tennant S., Buddles M., Curtis A., Goodship J.A. J. Med. Genet. 41:183-187(2004) [PubMed: 14985377] [Abstract] Cited for: INVOLVEMENT IN XELBD. |
| [6] | "Phosphoproteomic analysis of synaptosomes from human cerebral cortex." DeGiorgis J.A., Jaffe H., Moreira J.E., Carlotti C.G. Jr., Leite J.P., Pant H.C., Dosemeci A. J. Proteome Res. 4:306-315(2005) [PubMed: 15822905] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-427; SER-551; SER-553 AND SER-605, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [7] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-605, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| + | Additional computationally mapped references. |
Web resources
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M58378 M58377 Genomic DNA. Translation: AAC41930.1.M58378 M58377 Genomic DNA. Translation: AAC41931.1. Sequence problems.AL009172, Z84466 Genomic DNA. Translation: CAI42445.1. AL009172, Z84466 Genomic DNA. Translation: CAI42446.1. Z84466, AL009172 Genomic DNA. Translation: CAI42461.1. Z84466, AL009172 Genomic DNA. Translation: CAI42462.1. CH471164 Genomic DNA. Translation: EAW59313.1. M55301 Genomic DNA. Translation: AAA60608.1. |
| IPI | IPI00251507. IPI00300568. |
| PIR | A35363. |
| RefSeq | NP_008881.2. NM_006950.3. NP_598006.1. NM_133499.2. |
| UniGene | Hs.225936. |
3D structure databases | |
| ProteinModelPortal | P17600. |
| SMR | P17600. Positions 112-417. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P17600. 5 interactions. |
| MINT | MINT-1370745. |
| STRING | P17600. |
PTM databases | |
| PhosphoSite | P17600. |
Polymorphism databases | |
| DMDM | 73920800. |
Proteomic databases | |
| PRIDE | P17600. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000295987; ENSP00000295987; ENSG00000008056. |
| GeneID | 6853. |
| KEGG | hsa:6853. |
| UCSC | uc004did.1. human. uc004die.1. human. |
Organism-specific databases | |
| CTD | 6853. |
| GeneCards | GC0XM047431. |
| HGNC | HGNC:11494. SYN1. |
| HPA | CAB021929. HPA000397. |
| MIM | 300491. phenotype. 313440. gene. |
| neXtProt | NX_P17600. |
| Orphanet | 85294. X-linked epilepsy - learning disabilities - behavior disorders. |
| PharmGKB | PA36276. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG13995. |
| GeneTree | ENSGT00530000063319. |
| HOGENOM | HBG445598. |
| HOVERGEN | HBG016354. |
| InParanoid | P17600. |
| OMA | RNGVKVM. |
| PhylomeDB | P17600. |
Enzyme and pathway databases | |
| Reactome | REACT_13685. Neuronal System. |
Gene expression databases | |
| ArrayExpress | P17600. |
| Bgee | P17600. |
| CleanEx | HS_SYN1. |
| Genevestigator | P17600. |
| GermOnline | ENSG00000008056. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR013815. ATP_grasp_subdomain_1. IPR013816. ATP_grasp_subdomain_2. IPR013817. Pre-ATP_grasp. IPR016185. PreATP-grasp-like. IPR001359. Synapsin. IPR020898. Synapsin_ATP-bd_dom. IPR019735. Synapsin_CS. IPR019736. Synapsin_P_site. IPR020897. Synapsin_pre-ATP-grasp_dom. [Graphical view] |
| Gene3D | G3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit. G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 2 hits. G3DSA:3.40.50.20. Pre-ATP_grasp. 1 hit. |
| 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 | 26745. |
| SOURCE | Search... |
Entry information
| Entry name | SYN1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P17600 Secondary accession number(s): B1AJQ1, O75825, Q5H9A9 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

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