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P21579 (SYT1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Synaptotagmin-1
Alternative name(s):
Synaptotagmin I
Short name=SytI
p65
Gene names
Name:SYT1
Synonyms:SVP65, SYT
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May have a regulatory role in the membrane interactions during trafficking of synaptic vesicles at the active zone of the synapse. It binds acidic phospholipids with a specificity that requires the presence of both an acidic head group and a diacyl backbone. A Ca2+-dependent interaction between synaptotagmin and putative receptors for activated protein kinase C has also been reported. It can bind to at least three additional proteins in a Ca2+-independent manner; these are neurexins, syntaxin and AP2.

Cofactor

Binds 3 calcium ions per subunit. The ions are bound to the C2 domains By similarity.

Subunit structure

Homotetramer Probable. Interacts with SCAMP5, STON2, SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1 and SNAP25 By similarity. Ref.6

Subcellular location

Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesiclesecretory vesiclechromaffin granule membrane; Single-pass membrane protein. Cytoplasm. Note: Synaptic vesicles and chromaffin granules.

Domain

The first C2 domain mediates Ca2+-dependent phospholipid binding.

The second C2 domain mediates interaction with SV2A and STN2 By similarity.

Sequence similarities

Belongs to the synaptotagmin family.

Contains 2 C2 domains.

Ontologies

Keywords
   Cellular componentCell junction
Cytoplasm
Cytoplasmic vesicle
Membrane
Synapse
   DomainRepeat
Transmembrane
Transmembrane helix
   LigandCalcium
Metal-binding
   PTMGlycoprotein
Lipoprotein
Palmitate
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdetection of calcium ion

Traceable author statement PubMed 11438518. Source: UniProtKB

glutamate secretion

Traceable author statement. Source: Reactome

neurotransmitter secretion

Traceable author statement PubMed 11438518. Source: UniProtKB

positive regulation of calcium ion-dependent exocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of vesicle fusion

Inferred from electronic annotation. Source: Ensembl

protein homooligomerization

Traceable author statement PubMed 11438518. Source: UniProtKB

regulation of exocytosis

Traceable author statement PubMed 11438518. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

synaptic vesicle exocytosis

Inferred from electronic annotation. Source: Ensembl

vesicle docking

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

chromaffin granule membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

clathrin-sculpted acetylcholine transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted glutamate transport vesicle membrane

Traceable author statement. Source: Reactome

clathrin-sculpted monoamine transport vesicle membrane

Traceable author statement. Source: Reactome

dense core granule

Inferred from electronic annotation. Source: Ensembl

endocytic vesicle membrane

Traceable author statement. Source: Reactome

excitatory synapse

Inferred from electronic annotation. Source: Ensembl

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

neuron projection

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

presynaptic membrane

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle

Traceable author statement PubMed 11438518. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function1-phosphatidylinositol binding

Traceable author statement PubMed 11438518. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: Ensembl

calcium-dependent phospholipid binding

Inferred from electronic annotation. Source: Ensembl

low-density lipoprotein particle receptor binding

Inferred from direct assay PubMed 15082773. Source: MGI

phosphatidylinositol-4,5-bisphosphate binding

Inferred from electronic annotation. Source: Ensembl

phosphatidylserine binding

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Traceable author statement Ref.1. Source: ProtInc

syntaxin-1 binding

Traceable author statement PubMed 11438518. Source: UniProtKB

transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CACNB4O00305-22EBI-524909,EBI-714855
IKBKGQ9Y6K93EBI-524909,EBI-81279

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Synaptotagmin-1
PRO_0000183936

Regions

Topological domain1 – 5757Vesicular Potential
Transmembrane58 – 8023Helical; Potential
Topological domain81 – 422342Cytoplasmic Potential
Domain157 – 24589C2 1
Domain287 – 37892C2 2
Region136 – 382247Phospholipid binding Probable

Sites

Metal binding1721Calcium 2; via carbonyl oxygen By similarity
Metal binding1731Calcium 1 By similarity
Metal binding1731Calcium 2 By similarity
Metal binding1791Calcium 1 By similarity
Metal binding2311Calcium 1 By similarity
Metal binding2311Calcium 2 By similarity
Metal binding2321Calcium 1; via carbonyl oxygen By similarity
Metal binding2331Calcium 1 By similarity
Metal binding2331Calcium 2 By similarity
Metal binding2331Calcium 3 By similarity
Metal binding2361Calcium 3 By similarity
Metal binding2371Calcium 3; via carbonyl oxygen By similarity
Metal binding2391Calcium 2 By similarity
Metal binding2391Calcium 3 By similarity

Amino acid modifications

Modified residue1291Phosphothreonine Ref.7
Modified residue2301Phosphotyrosine By similarity
Lipidation751S-palmitoyl cysteine By similarity
Lipidation761S-palmitoyl cysteine By similarity
Lipidation781S-palmitoyl cysteine By similarity
Lipidation801S-palmitoyl cysteine By similarity
Lipidation831S-palmitoyl cysteine By similarity
Glycosylation251N-linked (GlcNAc...) Potential

Secondary structure

.................................................. 422
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P21579 [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 467F7C58E411AFA9

FASTA42247,573
        10         20         30         40         50         60 
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE LHKIPLPPWA 

        70         80         90        100        110        120 
LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN AINMKDVKDL GKTMKDQALK 

       130        140        150        160        170        180 
DDDAETGLTD GEEKEEPKEE EKLGKLQYSL DYDFQNNQLL VGIIQAAELP ALDMGGTSDP 

       190        200        210        220        230        240 
YVKVFLLPDK KKKFETKVHR KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI 

       250        260        270        280        290        300 
IGEFKVPMNT VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL 

       310        320        330        340        350        360 
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF EQIQKVQVVV 

       370        380        390        400        410        420 
TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR PIAQWHTLQV EEEVDAMLAV 


KK 

« Hide

References

« Hide 'large scale' references
[1]"Structural and functional conservation of synaptotagmin (p65) in Drosophila and humans."
Perin M.S., Johnston P.A., Oezcelik T., Jahn R., Francke U., Suedhof T.C.
J. Biol. Chem. 266:615-622(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Amygdala and Brain.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Hippocampus.
[4]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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: PNS.
[6]"Human SCAMP5, a novel secretory carrier membrane protein, facilitates calcium-triggered cytokine secretion by interaction with SNARE machinery."
Han C., Chen T., Yang M., Li N., Liu H., Cao X.
J. Immunol. 182:2986-2996(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SCAMP5.
[7]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M55047 mRNA. Translation: AAA60609.1.
AK094616 mRNA. Translation: BAG52897.1.
AK126908 mRNA. Translation: BAG54392.1.
CR627387 mRNA. Translation: CAH10483.1.
CH471054 Genomic DNA. Translation: EAW97343.1.
BC058917 mRNA. Translation: AAH58917.1.
PIRBMHU1Y. A39052.
RefSeqNP_001129277.1. NM_001135805.1.
NP_001129278.1. NM_001135806.1.
NP_005630.1. NM_005639.2.
UniGeneHs.310545.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2K45NMR-A141-268[»]
2K4ANMR-A141-268[»]
2K8MNMR-A/D141-268[»]
2KI6NMR-A/F141-268[»]
2LHANMR-A272-422[»]
2R83X-ray2.70A/B141-422[»]
3F00X-ray1.36A141-266[»]
3F01X-ray1.70A141-266[»]
3F04X-ray1.35A141-266[»]
3F05X-ray1.40A141-266[»]
4ISQX-ray2.65D/E/F33-53[»]
ProteinModelPortalP21579.
SMRP21579. Positions 141-419.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112723. 23 interactions.
DIPDIP-34042N.
IntActP21579. 16 interactions.
MINTMINT-1400342.
STRING9606.ENSP00000261205.

Protein family/group databases

TCDB1.F.1.1.1. the synaptosomal vesicle fusion pore (svf-pore) family.

PTM databases

PhosphoSiteP21579.

Polymorphism databases

DMDM135086.

Proteomic databases

PaxDbP21579.
PRIDEP21579.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261205; ENSP00000261205; ENSG00000067715.
ENST00000393240; ENSP00000376932; ENSG00000067715.
ENST00000552744; ENSP00000447575; ENSG00000067715.
GeneID6857.
KEGGhsa:6857.
UCSCuc001sys.3. human.

Organism-specific databases

CTD6857.
GeneCardsGC12P079232.
HGNCHGNC:11509. SYT1.
HPAHPA008394.
HPA064788.
MIM185605. gene.
neXtProtNX_P21579.
PharmGKBPA36290.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292488.
HOGENOMHOG000232127.
HOVERGENHBG005010.
InParanoidP21579.
KOK15290.
OMAHDIIGEY.
PhylomeDBP21579.
TreeFamTF315600.

Enzyme and pathway databases

ReactomeREACT_116125. Disease.
REACT_13685. Neuronal System.

Gene expression databases

ArrayExpressP21579.
BgeeP21579.
CleanExHS_SYT1.
GenevestigatorP21579.

Family and domain databases

Gene3D2.60.40.150. 2 hits.
InterProIPR000008. C2_dom.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1/2.
[Graphical view]
PANTHERPTHR10024:SF117. PTHR10024:SF117. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 2 hits.
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSYT1. human.
EvolutionaryTraceP21579.
GeneWikiSYT1.
GenomeRNAi6857.
NextBio26767.
PMAP-CutDBP21579.
PROP21579.
SOURCESearch...

Entry information

Entry nameSYT1_HUMAN
AccessionPrimary (citable) accession number: P21579
Secondary accession number(s): Q6AI31
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: April 16, 2014
This is version 152 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM