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Protein

Synapsin-1

Gene

Syn1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Neuronal phosphoprotein that coats synaptic vesicles, binds to the cytoskeleton, and is believed to function in the regulation of neurotransmitter release.

GO - Molecular functioni

  • ATP binding Source: InterPro
  • calcium-dependent protein binding Source: RGD
  • catalytic activity Source: InterPro

GO - Biological processi

  • neurotransmitter secretion Source: RGD
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Synapsin-1
Alternative name(s):
Synapsin I
Gene namesi
Name:Syn1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome X

Organism-specific databases

RGDi3797. Syn1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • cytosol Source: RGD
  • dendrite Source: BHF-UCL
  • Golgi apparatus Source: UniProtKB-SubCell
  • intracellular organelle Source: RGD
  • myelin sheath Source: Ensembl
  • postsynaptic density Source: Ensembl
  • presynaptic active zone Source: MGI
  • synapse Source: MGI
  • synaptic vesicle Source: UniProtKB
  • synaptic vesicle membrane Source: Ensembl
  • synaptonemal complex Source: Ensembl
  • terminal bouton Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Golgi apparatus, Synapse

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 704704Synapsin-1PRO_0000183020Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by CaMK1 and PKA1 Publication
Modified residuei39 – 391PhosphoserineCombined sources
Glycosylationi55 – 551O-linked (GlcNAc)2 Publications
Glycosylationi56 – 561O-linked (GlcNAc)1 Publication
Modified residuei62 – 621PhosphoserineCombined sources
Modified residuei67 – 671PhosphoserineCombined sources
Glycosylationi87 – 871O-linked (GlcNAc)2 Publications
Glycosylationi96 – 961O-linked (GlcNAc)1 Publication
Glycosylationi103 – 1031O-linked (GlcNAc)1 Publication
Glycosylationi261 – 2611O-linked (GlcNAc)1 Publication
Modified residuei312 – 3121PhosphotyrosineBy similarity
Modified residuei425 – 4251PhosphoserineCombined sources
Modified residuei430 – 4301Phosphoserine; alternateBy similarity
Glycosylationi430 – 4301O-linked (GlcNAc); alternate1 Publication
Modified residuei432 – 4321PhosphoserineBy similarity
Modified residuei434 – 4341PhosphothreonineCombined sources
Modified residuei436 – 4361PhosphoserineCombined sources
Glycosylationi516 – 5161O-linked (GlcNAc)2 Publications
Glycosylationi524 – 5241O-linked (GlcNAc)1 Publication
Modified residuei549 – 5491PhosphoserineBy similarity
Modified residuei551 – 5511Phosphoserine; by PDPK1By similarity
Glycosylationi562 – 5621O-linked (GlcNAc)1 Publication
Modified residuei566 – 5661PhosphoserineCombined sources
Modified residuei566 – 5661Phosphoserine; by CaMK21 Publication
Glycosylationi576 – 5761O-linked (GlcNAc)1 Publication
Modified residuei603 – 6031Phosphoserine; by CaMK21 Publication
Modified residuei662 – 6621PhosphoserineBy similarity
Modified residuei664 – 6641PhosphoserineCombined sources
Modified residuei682 – 6821PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP09951.
PRIDEiP09951.

PTM databases

iPTMnetiP09951.
PhosphoSiteiP09951.

Expressioni

Gene expression databases

GenevisibleiP09951. RN.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with CAPON. Forms a ternary complex with NOS1. Isoform Ib interacts with PRNP (By similarity).By similarity

GO - Molecular functioni

  • calcium-dependent protein binding Source: RGD

Protein-protein interaction databases

BioGridi247051. 1 interaction.
IntActiP09951. 5 interactions.
MINTiMINT-139278.
STRINGi10116.ENSRNOP00000014250.

Structurei

Secondary structure

1
704
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi114 – 1196Combined sources
Helixi126 – 1305Combined sources
Turni136 – 1383Combined sources
Beta strandi139 – 1468Combined sources
Helixi148 – 1503Combined sources
Beta strandi151 – 1566Combined sources
Beta strandi161 – 1699Combined sources
Beta strandi172 – 1787Combined sources
Beta strandi181 – 1855Combined sources
Helixi199 – 2079Combined sources
Beta strandi212 – 2143Combined sources
Helixi216 – 2216Combined sources
Helixi225 – 23915Combined sources
Turni241 – 2433Combined sources
Beta strandi250 – 2545Combined sources
Helixi255 – 2573Combined sources
Beta strandi262 – 27211Combined sources
Turni275 – 2784Combined sources
Beta strandi279 – 2824Combined sources
Helixi285 – 29814Combined sources
Beta strandi302 – 3065Combined sources
Beta strandi310 – 31910Combined sources
Beta strandi322 – 33312Combined sources
Beta strandi342 – 3476Combined sources
Helixi351 – 36010Combined sources
Helixi361 – 3655Combined sources
Beta strandi368 – 37710Combined sources
Beta strandi382 – 3887Combined sources
Helixi396 – 3983Combined sources
Helixi399 – 41517Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK8X-ray2.10A/B/C/D/E/F/G/H2-421[»]
1PX2X-ray2.23A/B2-421[»]
ProteinModelPortaliP09951.
SMRiP09951. Positions 112-417.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP09951.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2828AAdd
BLAST
Regioni29 – 11284B; linkerAdd
BLAST
Regioni113 – 420308C; actin-binding and synaptic-vesicle bindingAdd
BLAST
Regioni421 – 655235D; Pro-rich linkerAdd
BLAST
Regioni656 – 70449EAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the synapsin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3895. Eukaryota.
ENOG410XQH5. LUCA.
GeneTreeiENSGT00530000063319.
HOGENOMiHOG000231323.
HOVERGENiHBG016354.
InParanoidiP09951.
KOiK19941.
OMAiPIRQASQ.
OrthoDBiEOG793B7G.
PhylomeDBiP09951.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProiIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR028713. SYN1.
IPR001359. Synapsin.
IPR020898. Synapsin_ATP-bd_dom.
IPR019735. Synapsin_CS.
IPR019736. Synapsin_P_site.
IPR020897. Synapsin_pre-ATP-grasp_dom.
[Graphical view]
PANTHERiPTHR10841. PTHR10841. 2 hits.
PTHR10841:SF22. PTHR10841:SF22. 2 hits.
PfamiPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSiPR01368. SYNAPSIN.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform IA (identifier: P09951-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPSAASP GATPGSAAAS
60 70 80 90 100
AERASTAAPV ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG
110 120 130 140 150
GGSGGAGRGG AAARVLLVID EPHTDWAKYF KGKKIHGEID IKVEQAEFSD
160 170 180 190 200
LNLVAHANGG FSVDMEVLRN GVKVVRSLKP DFVLIRQHAF SMARNGDYRS
210 220 230 240 250
LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG TEEFPLIDQT
260 270 280 290 300
FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
310 320 330 340 350
YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS
360 370 380 390 400
DRYKLWVDTC SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD
410 420 430 440 450
EDKQLIVELV VNKMTQALPR QRDASPGRGS HSQTPSPGAL PLGRQTSQQP
460 470 480 490 500
AGPPAQQRPP PQGGPPQPGP GPQRQGPPLQ QRPPPQGQQH LSGLGPPAGS
510 520 530 540 550
PLPQRLPSPT AAPQQSASQA TPMTQGQGRQ SRPVAGGPGA PPAARPPASP
560 570 580 590 600
SPQRQAGPPQ ATRQASISGP APPKVSGASP GGQQRQGPPQ KPPGPAGPIR
610 620 630 640 650
QASQAGPGPR TGPPTTQQPR PSGPGPAGRP TKPQLAQKPS QDVPPPIIAA
660 670 680 690 700
AGGPPHPQLN KSQSLTNAFN LPEPAPPRPS LSQDEVKAET IRSLRKSFAS

LFSD
Length:704
Mass (Da):73,988
Last modified:May 30, 2000 - v3
Checksum:i65799FEF7CFE18B5
GO
Isoform IB (identifier: P09951-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     660-668: NKSQSLTNA → KASPAQAQP
     669-704: Missing.

Show »
Length:668
Mass (Da):69,910
Checksum:iCE225AE8FCC92F8F
GO

Sequence cautioni

The sequence CAA28353.1 differs from that shown.Sequencing errors.Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei660 – 6689NKSQSLTNA → KASPAQAQP in isoform IB. CuratedVSP_006318
Alternative sequencei669 – 70436Missing in isoform IB. CuratedVSP_006319Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27812 mRNA. Translation: AAA42145.1.
M27924 mRNA. Translation: AAA42148.1.
X04655 mRNA. Translation: CAA28353.1. Sequence problems.
PIRiA25704.
A30411.
RefSeqiNP_001104252.1. NM_001110782.2. [P09951-2]
NP_062006.1. NM_019133.2. [P09951-1]
UniGeneiRn.9923.

Genome annotation databases

EnsembliENSRNOT00000014250; ENSRNOP00000014250; ENSRNOG00000010365. [P09951-1]
GeneIDi24949.
KEGGirno:24949.
UCSCiRGD:3797. rat. [P09951-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M27812 mRNA. Translation: AAA42145.1.
M27924 mRNA. Translation: AAA42148.1.
X04655 mRNA. Translation: CAA28353.1. Sequence problems.
PIRiA25704.
A30411.
RefSeqiNP_001104252.1. NM_001110782.2. [P09951-2]
NP_062006.1. NM_019133.2. [P09951-1]
UniGeneiRn.9923.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PK8X-ray2.10A/B/C/D/E/F/G/H2-421[»]
1PX2X-ray2.23A/B2-421[»]
ProteinModelPortaliP09951.
SMRiP09951. Positions 112-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247051. 1 interaction.
IntActiP09951. 5 interactions.
MINTiMINT-139278.
STRINGi10116.ENSRNOP00000014250.

PTM databases

iPTMnetiP09951.
PhosphoSiteiP09951.

Proteomic databases

PaxDbiP09951.
PRIDEiP09951.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000014250; ENSRNOP00000014250; ENSRNOG00000010365. [P09951-1]
GeneIDi24949.
KEGGirno:24949.
UCSCiRGD:3797. rat. [P09951-1]

Organism-specific databases

CTDi6853.
RGDi3797. Syn1.

Phylogenomic databases

eggNOGiKOG3895. Eukaryota.
ENOG410XQH5. LUCA.
GeneTreeiENSGT00530000063319.
HOGENOMiHOG000231323.
HOVERGENiHBG016354.
InParanoidiP09951.
KOiK19941.
OMAiPIRQASQ.
OrthoDBiEOG793B7G.
PhylomeDBiP09951.

Miscellaneous databases

EvolutionaryTraceiP09951.
PROiP09951.

Gene expression databases

GenevisibleiP09951. RN.

Family and domain databases

Gene3Di3.30.1490.20. 1 hit.
3.30.470.20. 2 hits.
3.40.50.20. 1 hit.
InterProiIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR016185. PreATP-grasp_dom.
IPR028713. SYN1.
IPR001359. Synapsin.
IPR020898. Synapsin_ATP-bd_dom.
IPR019735. Synapsin_CS.
IPR019736. Synapsin_P_site.
IPR020897. Synapsin_pre-ATP-grasp_dom.
[Graphical view]
PANTHERiPTHR10841. PTHR10841. 2 hits.
PTHR10841:SF22. PTHR10841:SF22. 2 hits.
PfamiPF02078. Synapsin. 1 hit.
PF02750. Synapsin_C. 1 hit.
PF10581. Synapsin_N. 1 hit.
[Graphical view]
PRINTSiPR01368. SYNAPSIN.
SUPFAMiSSF52440. SSF52440. 1 hit.
PROSITEiPS00415. SYNAPSIN_1. 1 hit.
PS00416. SYNAPSIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Synapsins: mosaics of shared and individual domains in a family of synaptic vesicle phosphoproteins."
    Suedhof T.C., Czernik A.J., Kao H.-T., Takei K., Johnston P.A., Horiuchi A., Kanazir S.D., Wagner M.A., Perin M.S., de Camilli P., Greengard P.
    Science 245:1474-1480(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  2. "Determination and analysis of the primary structure of the nerve terminal specific phosphoprotein, synapsin I."
    McCaffery C.A., Degennaro L.J.
    EMBO J. 5:3167-3173(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. Lubec G., Diao W.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 177-186 AND 239-256, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Amino acid sequences surrounding the cAMP-dependent and calcium/calmodulin-dependent phosphorylation sites in rat and bovine synapsin I."
    Czernik A.J., Pang D.T., Greengard P.
    Proc. Natl. Acad. Sci. U.S.A. 84:7518-7522(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-566 AND SER-603.
  5. "Glycosylation sites flank phosphorylation sites on synapsin I: O-linked N-acetylglucosamine residues are localized within domains mediating synapsin I interactions."
    Cole R.N., Hart G.W.
    J. Neurochem. 73:418-428(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-55; THR-56; THR-87; SER-516; THR-524; THR-562 AND SER-576.
  6. "A phospho-switch controls the dynamic association of synapsins with synaptic vesicles."
    Hosaka M., Hammer R.E., Sudhof T.C.
    Neuron 24:377-387(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-9.
  7. "Mapping sites of O-GlcNAc modification using affinity tags for serine and threonine post-translational modifications."
    Wells L., Vosseller K., Cole R.N., Cronshaw J.M., Matunis M.J., Hart G.W.
    Mol. Cell. Proteomics 1:791-804(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT SER-55; THR-87; SER-96; SER-103; SER-261; SER-430 AND SER-516.
  8. "Neuronal nitric-oxide synthase localization mediated by a ternary complex with synapsin and CAPON."
    Jaffrey S.R., Benfenati F., Snowman A.M., Czernik A.J., Snyder S.H.
    Proc. Natl. Acad. Sci. U.S.A. 99:3199-3204(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NOS1 AND CAPON.
  9. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-62; SER-67; SER-425; THR-434; SER-436; SER-566 AND SER-664, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSYN1_RAT
AccessioniPrimary (citable) accession number: P09951
Secondary accession number(s): Q9WUX7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 30, 2000
Last modified: June 8, 2016
This is version 146 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.