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Q8JZP2 (SYN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synapsin-3
Alternative name(s):
Synapsin III
Gene names
Name:Syn3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length579 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be involved in the regulation of neurotransmitter release and synaptogenesis. Binds ATP with high affinity and ADP with a lower affinity. This is consistent with a catalytic role of the C-domain in which ADP would be dissociated by cellular ATP after bound ATP was hydrolyzed By similarity.

Subunit structure

Interacts with CAPON By similarity.

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Peripheral membrane protein localized to the cytoplasmic surface of synaptic vesicles By similarity.

Domain

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

Post-translational modification

Phosphorylation at Ser-9 dissociates synapsins from synaptic vesicles By similarity.

Miscellaneous

Regulated by calcium. Calcium inhibits ATP binding to the C-domain By similarity.

Sequence similarities

Belongs to the synapsin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 579579Synapsin-3
PRO_0000183025

Regions

Region1 – 2828A
Region28 – 9063B; linker
Region91 – 398308C; actin-binding and synaptic-vesicle binding
Region399 – 530132J; Pro-rich linker
Region531 – 57949E

Amino acid modifications

Modified residue91Phosphoserine; by PKA and CaMK1 By similarity
Modified residue4691Phosphoserine; by CDK1 and MAPK By similarity
Modified residue4831Phosphoserine Ref.3

Experimental info

Sequence conflict651G → S in AAM22969. Ref.1
Sequence conflict651G → S in AAM22970. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8JZP2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2B84E36A1663D50F

FASTA57963,315
        10         20         30         40         50         60 
MNFLRRRLSD SSFVANLPNG YMPDLQRPES SSSSPASPAT ERRHPQPLAA SFSSPGSSLF 

        70         80         90        100        110        120 
SSFSGAMKQT PQAPSGLMEP PTPVTPVVQR PRILLVIDDA HTDWSKYFHG KKVNGDIEIR 

       130        140        150        160        170        180 
VEQAEFSELN LAAYVTGGCM VDMQVVRNGT KIVRSFKPDF ILVRQHAYSM ALAEDYRSLV 

       190        200        210        220        230        240 
IGLQYGGLPA VNSLYSVYNF CSKPWVFSQL IKIFHSLGPE KFPLVEQTFF PNHKPMLTAP 

       250        260        270        280        290        300 
NFPVVIKLGH AHAGMGKIKV ENQHDYQDIT SVVAMAKTYA TTEAFIDSKY DIRIQKIGSN 

       310        320        330        340        350        360 
YKAYMRTSIS GNWKANTGSA MLEQVAMTER YRLWVDSCSE MFGGLDICAV KAVHSKDGRD 

       370        380        390        400        410        420 
YIIEVMDSSM PLIGEHVEED KQLMADLVVS KMSQLLVPGA TVPSPLRPWG PQTKPAKSPG 

       430        440        450        460        470        480 
QGQLGPLLGQ PQPRPPPQGG PRQAQSPQPP RSRSPSQQRL SPQGQQPVSP QSGSPQQQRS 

       490        500        510        520        530        540 
PGSPQLSRAS GGSSPNQASK PSASLSSHNR PPVQGRSTSQ QGEEPQKSAS PHPHLNKSQS 

       550        560        570 
LTNSLSTSDT SHRGTPSEDE AKAETIRNLR KSFASLFSD 

« Hide

References

« Hide 'large scale' references
[1]"High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: ILS and ISS.
[2]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[3]"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-483, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain.
[4]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF498252 mRNA. Translation: AAM22969.1.
AF498253 mRNA. Translation: AAM22970.1.
AC122919 Genomic DNA. No translation available.
AC124614 Genomic DNA. No translation available.
AC125060 Genomic DNA. No translation available.
AC145076 Genomic DNA. No translation available.
AC150899 Genomic DNA. No translation available.
CCDSCCDS24096.1.
RefSeqNP_038750.2. NM_013722.3.
XP_006513761.1. XM_006513698.1.
XP_006513762.1. XM_006513699.1.
XP_006513763.1. XM_006513700.1.
UniGeneMm.394931.
Mm.444790.

3D structure databases

ProteinModelPortalQ8JZP2.
SMRQ8JZP2. Positions 90-395.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid205126. 1 interaction.
IntActQ8JZP2. 2 interactions.
MINTMINT-4136325.

PTM databases

PhosphoSiteQ8JZP2.

Proteomic databases

MaxQBQ8JZP2.
PaxDbQ8JZP2.
PRIDEQ8JZP2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000120638; ENSMUSP00000113720; ENSMUSG00000059602.
GeneID27204.
KEGGmmu:27204.
UCSCuc007gnn.2. mouse.

Organism-specific databases

CTD8224.
MGIMGI:1351334. Syn3.

Phylogenomic databases

eggNOGNOG284201.
GeneTreeENSGT00530000063319.
HOGENOMHOG000231323.
HOVERGENHBG016354.
InParanoidQ8JZP2.
OMANHKPMLT.
OrthoDBEOG793B7G.
TreeFamTF319919.

Gene expression databases

BgeeQ8JZP2.
CleanExMM_SYN3.
GenevestigatorQ8JZP2.

Family and domain databases

Gene3D3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProIPR013815. 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]
PANTHERPTHR10841. PTHR10841. 1 hit.
PfamPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSPR01368. SYNAPSIN.
SUPFAMSSF52440. SSF52440. 1 hit.
PROSITEPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYN3. mouse.
NextBio305067.
PROQ8JZP2.
SOURCESearch...

Entry information

Entry nameSYN3_MOUSE
AccessionPrimary (citable) accession number: Q8JZP2
Secondary accession number(s): E9QNQ6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 11, 2004
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 92 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot