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Reviewed, UniProtKB/Swiss-Prot P21579 (SYT1_HUMAN)

Last modified November 3, 2009. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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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) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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, STN2, SV2A, SV2B, SV2C and RIMS1. Forms a complex with SV2B, syntaxin 1 and SNAP25 By similarity.

Subcellular location

Cytoplasmic vesicle › secretory vesicle › synaptic vesicle membrane; Single-pass membrane protein. Cytoplasmic vesicle › secretory vesicle › chromaffin 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.

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

CACNB4O00305-21EBI-524909,EBI-714855

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 422422Synaptotagmin-1
PRO_0000183936

Regions

Topological domain1 – 5757Vesicular Potential
Transmembrane58 – 8023 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 By similarity
Modified residue2301Phosphotyrosine By similarity
Modified residue2371N6-acetyllysine Ref.4
Modified residue3651Phosphotyrosine By similarity
Modified residue3811Phosphotyrosine 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

1 .............................................. 422
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P21579-1 [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

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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: 1840599] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: PNS.
[3]"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: 19234194] [Abstract]
Cited for: INTERACTION WITH SCAMP5.
[4]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-237, MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

M55047 mRNA. Translation: AAA60609.1.
BC058917 mRNA. Translation: AAH58917.1.
IPIIPI00009439.
PIRBMHU1Y. A39052.
RefSeqNP_001129277.1.
NP_001129278.1.
NP_005630.1.
UniGeneHs.310545

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2K45NMR-A141-268[»]
2K4ANMR-A141-268[»]
2K8MNMR-A/D141-268[»]
2R83X-ray2.70A/B141-422[»]
3F00X-ray1.36A141-266[»]
3F04X-ray1.35A141-266[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP21579. 8 interactions.
STRINGP21579.

PTM databases

PhosphoSiteP21579.

Proteomic databases

PRIDEP21579.

Genome annotation databases

EnsemblENST00000261205; ENSP00000261205; ENSG00000067715; Homo sapiens. [Genome view]
ENST00000393240; ENSP00000376932; ENSG00000067715; Homo sapiens. [Genome view]
ENST00000446242; ENSP00000401559; ENSG00000067715; Homo sapiens. [Genome view]
ENST00000457153; ENSP00000391056; ENSG00000067715; Homo sapiens. [Genome view]
GeneID6857.
KEGGhsa:6857.
UCSCuc001sys.1. human.

Organism-specific databases

CTD6857.
GeneCardsGC12P077760.
H-InvDBHIX0010846.
HGNCHGNC:11509. SYT1.
HPAHPA008394.
MIM185605. gene.
PharmGKBPA36290.
GenAtlasSearch...

Phylogenomic databases

HOGENOMP21579.
HOVERGENP21579.
OMAVPHNATE.

Enzyme and pathway databases

ReactomeREACT_11184. Botulinum neurotoxicity.
REACT_13685. Synaptic Transmission.

Gene expression databases

ArrayExpressP21579.
BgeeP21579.
CleanExHS_SYT1.
GenevestigatorP21579.
GermOnlineENSG00000067715. Homo sapiens.

Family and domain databases

InterProIPR000008. C2_Ca-dep.
IPR018029. C2_membr_targeting.
IPR020477. C2_region.
IPR001565. Synaptotagmin.
IPR015428. Synaptotagmin1_2.
[Graphical view]
PANTHERPTHR10024:SF39. Synaptotagmin1_2. 1 hit.
PfamPF00168. C2. 2 hits.
[Graphical view]
PRINTSPR00360. C2DOMAIN.
PR00399. SYNAPTOTAGMN.
SMARTSM00239. C2. 2 hits.
[Graphical view]
PROSITEPS50004. C2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio26767.
PMAP-CutDBP21579.
SOURCESearch...

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Entry information

Entry nameSYT1_HUMAN
AccessionPrimary (citable) accession number: P21579
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: November 3, 2009
This is version 110 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 12

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

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents