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Protein

Synapsin-3

Gene

SYN3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be involved in the regulation of neurotransmitter release and synaptogenesis.

GO - Molecular functioni

  • ATP binding Source: ParkinsonsUK-UCL
  • catalytic activity Source: InterPro

GO - Biological processi

  • neurotransmitter secretion Source: ProtInc
  • regulation of synaptic transmission, GABAergic Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Calcium, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-181429. Serotonin Neurotransmitter Release Cycle.
R-HSA-212676. Dopamine Neurotransmitter Release Cycle.
SIGNORiO14994.

Names & Taxonomyi

Protein namesi
Recommended name:
Synapsin-3
Alternative name(s):
Synapsin III
Gene namesi
Name:SYN3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:11496. SYN3.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB-KW
  • neuronal postsynaptic density Source: Ensembl
  • synaptic vesicle Source: ProtInc
  • synaptic vesicle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasmic vesicle, Membrane, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36278.

Polymorphism and mutation databases

BioMutaiSYN3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 580580Synapsin-3PRO_0000183024Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine; by PKA and CaMK1By similarity
Modified residuei455 – 4551PhosphoserineBy similarity
Modified residuei462 – 4621PhosphoserineBy similarity
Modified residuei470 – 4701Phosphoserine; by CDK1 and MAPK1 Publication
Modified residuei475 – 4751PhosphoserineBy similarity
Modified residuei481 – 4811PhosphoserineBy similarity
Modified residuei484 – 4841PhosphoserineBy similarity
Modified residuei541 – 5411PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiO14994.
PRIDEiO14994.

PTM databases

iPTMnetiO14994.
PhosphoSiteiO14994.

Expressioni

Tissue specificityi

Neuron specific. Detected predominantly in brain.

Gene expression databases

BgeeiO14994.
CleanExiHS_SYN3.
ExpressionAtlasiO14994. baseline and differential.
GenevisibleiO14994. HS.

Organism-specific databases

HPAiHPA034566.

Interactioni

Subunit structurei

Interacts with CAPON.By similarity

Protein-protein interaction databases

BioGridi113857. 2 interactions.
STRINGi9606.ENSP00000330219.

Structurei

Secondary structure

1
580
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi92 – 976Combined sources
Helixi104 – 1085Combined sources
Turni114 – 1163Combined sources
Beta strandi117 – 1248Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1346Combined sources
Beta strandi139 – 1435Combined sources
Beta strandi160 – 1645Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 1733Combined sources
Helixi178 – 1869Combined sources
Beta strandi191 – 1933Combined sources
Helixi195 – 2006Combined sources
Helixi204 – 21815Combined sources
Turni220 – 2223Combined sources
Beta strandi229 – 2346Combined sources
Beta strandi241 – 25111Combined sources
Turni254 – 2574Combined sources
Beta strandi258 – 2614Combined sources
Helixi264 – 27714Combined sources
Beta strandi281 – 2855Combined sources
Beta strandi289 – 29810Combined sources
Beta strandi301 – 31212Combined sources
Beta strandi318 – 3269Combined sources
Helixi330 – 33910Combined sources
Helixi340 – 3445Combined sources
Beta strandi347 – 35610Combined sources
Beta strandi361 – 3677Combined sources
Helixi375 – 3773Combined sources
Helixi378 – 39417Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0AX-ray1.90A/B76-417[»]
ProteinModelPortaliO14994.
SMRiO14994. Positions 90-397.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO14994.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 2828AAdd
BLAST
Regioni28 – 9063B; linkerAdd
BLAST
Regioni91 – 399309C; actin-binding and synaptic-vesicle bindingAdd
BLAST
Regioni400 – 531132J; Pro-rich linkerAdd
BLAST
Regioni532 – 58049EAdd
BLAST

Domaini

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

Sequence similaritiesi

Belongs to the synapsin family.Curated

Phylogenomic databases

eggNOGiKOG3895. Eukaryota.
ENOG410XQH5. LUCA.
GeneTreeiENSGT00530000063319.
HOVERGENiHBG016354.
InParanoidiO14994.
KOiK19941.
OMAiNHKPMLT.
OrthoDBiEOG793B7G.
PhylomeDBiO14994.
TreeFamiTF319919.

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.
IPR001359. Synapsin.
IPR020898. Synapsin_ATP-bd_dom.
IPR019735. Synapsin_CS.
IPR019736. Synapsin_P_site.
IPR020897. Synapsin_pre-ATP-grasp_dom.
[Graphical view]
PANTHERiPTHR10841. PTHR10841. 1 hit.
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]

Sequencei

Sequence statusi: Complete.

O14994-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNFLRRRLSD SSFMANLPNG YMTDLQRPDS STSSPASPAM ERRHPQPLAA
60 70 80 90 100
SFSSPGSSLF SSLSSAMKQA PQATSGLMEP PGPSTPIVQR PRILLVIDDA
110 120 130 140 150
HTDWSKYFHG KKVNGEIEIR VEQAEFSELN LAAYVTGGCM VDMQVVRNGT
160 170 180 190 200
KVVSRSFKPD FILVRQHAYS MALGEDYRSL VIGLQYGGLP AVNSLYSVYN
210 220 230 240 250
FCSKPWVFSQ LIKIFHSLGP EKFPLVEQTF FPNHKPMVTA PHFPVVVKLG
260 270 280 290 300
HAHAGMGKIK VENQLDFQDI TSVVAMAKTY ATTEAFIDSK YDIRIQKIGS
310 320 330 340 350
NYKAYMRTSI SGNWKANTGS AMLEQVAMTE RYRLWVDSCS EMFGGLDICA
360 370 380 390 400
VKAVHSKDGR DYIIEVMDSS MPLIGEHVEE DRQLMADLVV SKMSQLPMPG
410 420 430 440 450
GTAPSPLRPW APQIKSAKSP GQAQLGPQLG QPQPRPPPQG GPRQAQSPQP
460 470 480 490 500
QRSGSPSQQR LSPQGQQPLS PQSGSPQQQR SPGSPQLSRA SSGSSPNQAS
510 520 530 540 550
KPGATLASQP RPPVQGRSTS QQGEESKKPA PPHPHLNKSQ SLTNSLSTSD
560 570 580
TSQRGTPSED EAKAETIRNL RKSFASLFSD
Length:580
Mass (Da):63,303
Last modified:November 1, 1998 - v2
Checksum:i4F61DE236DE8F3C5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti470 – 4701S → N in patients affected by schizophrenia. 1 Publication
Corresponds to variant rs5998526 [ dbSNP | Ensembl ].
VAR_068906

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046873 mRNA. Translation: AAC15101.1.
CR456589 mRNA. Translation: CAG30475.1.
Z83846
, Z71183, Z80902, Z82181, Z82246, Z98256 Genomic DNA. Translation: CAB62947.2.
Z71183
, Z80902, Z82181, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAB63144.2.
Z98256
, Z71183, Z80902, Z82181, Z82246, Z83846 Genomic DNA. Translation: CAB10915.2.
Z82181
, Z71183, Z80902, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAI18771.1.
Z82246
, Z71183, Z80902, Z82181, Z83846, Z98256 Genomic DNA. Translation: CAI18775.1.
Z80902
, Z71183, Z82181, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAI18794.1.
CH471095 Genomic DNA. Translation: EAW60034.1.
BC075065 mRNA. Translation: AAH75065.1.
BC075066 mRNA. Translation: AAH75066.1.
BC143874 mRNA. Translation: AAI43875.1.
CCDSiCCDS13908.1.
RefSeqiNP_003481.3. NM_003490.3.
NP_598344.2. NM_133633.2.
XP_011528707.1. XM_011530405.1.
XP_011528708.1. XM_011530406.1.
XP_011528709.1. XM_011530407.1.
XP_011528710.1. XM_011530408.1.
XP_011528711.1. XM_011530409.1.
UniGeneiHs.608750.

Genome annotation databases

EnsembliENST00000358763; ENSP00000351614; ENSG00000185666.
GeneIDi8224.
KEGGihsa:8224.
UCSCiuc003amx.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF046873 mRNA. Translation: AAC15101.1.
CR456589 mRNA. Translation: CAG30475.1.
Z83846
, Z71183, Z80902, Z82181, Z82246, Z98256 Genomic DNA. Translation: CAB62947.2.
Z71183
, Z80902, Z82181, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAB63144.2.
Z98256
, Z71183, Z80902, Z82181, Z82246, Z83846 Genomic DNA. Translation: CAB10915.2.
Z82181
, Z71183, Z80902, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAI18771.1.
Z82246
, Z71183, Z80902, Z82181, Z83846, Z98256 Genomic DNA. Translation: CAI18775.1.
Z80902
, Z71183, Z82181, Z82246, Z83846, Z98256 Genomic DNA. Translation: CAI18794.1.
CH471095 Genomic DNA. Translation: EAW60034.1.
BC075065 mRNA. Translation: AAH75065.1.
BC075066 mRNA. Translation: AAH75066.1.
BC143874 mRNA. Translation: AAI43875.1.
CCDSiCCDS13908.1.
RefSeqiNP_003481.3. NM_003490.3.
NP_598344.2. NM_133633.2.
XP_011528707.1. XM_011530405.1.
XP_011528708.1. XM_011530406.1.
XP_011528709.1. XM_011530407.1.
XP_011528710.1. XM_011530408.1.
XP_011528711.1. XM_011530409.1.
UniGeneiHs.608750.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P0AX-ray1.90A/B76-417[»]
ProteinModelPortaliO14994.
SMRiO14994. Positions 90-397.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113857. 2 interactions.
STRINGi9606.ENSP00000330219.

PTM databases

iPTMnetiO14994.
PhosphoSiteiO14994.

Polymorphism and mutation databases

BioMutaiSYN3.

Proteomic databases

PaxDbiO14994.
PRIDEiO14994.

Protocols and materials databases

DNASUi8224.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358763; ENSP00000351614; ENSG00000185666.
GeneIDi8224.
KEGGihsa:8224.
UCSCiuc003amx.4. human.

Organism-specific databases

CTDi8224.
GeneCardsiSYN3.
HGNCiHGNC:11496. SYN3.
HPAiHPA034566.
MIMi602705. gene.
neXtProtiNX_O14994.
PharmGKBiPA36278.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3895. Eukaryota.
ENOG410XQH5. LUCA.
GeneTreeiENSGT00530000063319.
HOVERGENiHBG016354.
InParanoidiO14994.
KOiK19941.
OMAiNHKPMLT.
OrthoDBiEOG793B7G.
PhylomeDBiO14994.
TreeFamiTF319919.

Enzyme and pathway databases

ReactomeiR-HSA-181429. Serotonin Neurotransmitter Release Cycle.
R-HSA-212676. Dopamine Neurotransmitter Release Cycle.
SIGNORiO14994.

Miscellaneous databases

ChiTaRSiSYN3. human.
EvolutionaryTraceiO14994.
GeneWikiiSYN3.
GenomeRNAii8224.
PROiO14994.
SOURCEiSearch...

Gene expression databases

BgeeiO14994.
CleanExiHS_SYN3.
ExpressionAtlasiO14994. baseline and differential.
GenevisibleiO14994. HS.

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.
IPR001359. Synapsin.
IPR020898. Synapsin_ATP-bd_dom.
IPR019735. Synapsin_CS.
IPR019736. Synapsin_P_site.
IPR020897. Synapsin_pre-ATP-grasp_dom.
[Graphical view]
PANTHERiPTHR10841. PTHR10841. 1 hit.
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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain.
  6. "A rare polymorphism affects a mitogen-activated protein kinase site in synapsin III: possible relationship to schizophrenia."
    Porton B., Ferreira A., DeLisi L.E., Kao H.T.
    Biol. Psychiatry 55:118-125(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-470, VARIANT ASN-470.

Entry informationi

Entry nameiSYN3_HUMAN
AccessioniPrimary (citable) accession number: O14994
Secondary accession number(s): B1B1F9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1998
Last modified: June 8, 2016
This is version 148 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.