CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004983
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Synaptotagmin-1 
Protein Synonyms/Alias
 Synaptotagmin I; SytI; p65 
Gene Name
 SYT1 
Gene Synonyms/Alias
 SVP65; SYT 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
105GKNAINMKDVKDLGKubiquitination[1]
120TMKDQALKDDDAETGubiquitination[1, 2]
134GLTDGEEKEEPKEEEubiquitination[1, 2]
237YDFDRFSKHDIIGEFacetylation[3]
268RDLQSAEKEEQEKLGubiquitination[1]
333KKKTTIKKNTLNPYYubiquitination[1, 2]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861] 
Functional Description
 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 Ca(2+)-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 Ca(2+)-independent manner; these are neurexins, syntaxin and AP2. 
Sequence Annotation
 DOMAIN 157 245 C2 1.
 DOMAIN 287 378 C2 2.
 REGION 136 382 Phospholipid binding (Probable).
 METAL 172 172 Calcium 2; via carbonyl oxygen (By
 METAL 173 173 Calcium 1 (By similarity).
 METAL 173 173 Calcium 2 (By similarity).
 METAL 179 179 Calcium 1 (By similarity).
 METAL 231 231 Calcium 1 (By similarity).
 METAL 231 231 Calcium 2 (By similarity).
 METAL 232 232 Calcium 1; via carbonyl oxygen (By
 METAL 233 233 Calcium 1 (By similarity).
 METAL 233 233 Calcium 2 (By similarity).
 METAL 233 233 Calcium 3 (By similarity).
 METAL 236 236 Calcium 3 (By similarity).
 METAL 237 237 Calcium 3; via carbonyl oxygen (By
 METAL 239 239 Calcium 2 (By similarity).
 METAL 239 239 Calcium 3 (By similarity).
 MOD_RES 129 129 Phosphothreonine.
 MOD_RES 230 230 Phosphotyrosine (By similarity).
 MOD_RES 365 365 Phosphotyrosine (By similarity).
 MOD_RES 381 381 Phosphotyrosine (By similarity).
 LIPID 75 75 S-palmitoyl cysteine (By similarity).
 LIPID 76 76 S-palmitoyl cysteine (By similarity).
 LIPID 78 78 S-palmitoyl cysteine (By similarity).
 LIPID 80 80 S-palmitoyl cysteine (By similarity).
 LIPID 83 83 S-palmitoyl cysteine (By similarity).
 CARBOHYD 25 25 N-linked (GlcNAc...) (Potential).  
Keyword
 3D-structure; Calcium; Cell junction; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 422 AA 
Protein Sequence
MVSESHHEAL AAPPVTTVAT VLPSNATEPA SPGEGKEDAF SKLKEKFMNE LHKIPLPPWA 60
LIAIAIVAVL LVLTCCFCIC KKCLFKKKNK KKGKEKGGKN AINMKDVKDL GKTMKDQALK 120
DDDAETGLTD GEEKEEPKEE EKLGKLQYSL DYDFQNNQLL VGIIQAAELP ALDMGGTSDP 180
YVKVFLLPDK KKKFETKVHR KTLNPVFNEQ FTFKVPYSEL GGKTLVMAVY DFDRFSKHDI 240
IGEFKVPMNT VDFGHVTEEW RDLQSAEKEE QEKLGDICFS LRYVPTAGKL TVVILEAKNL 300
KKMDVGGLSD PYVKIHLMQN GKRLKKKKTT IKKNTLNPYY NESFSFEVPF EQIQKVQVVV 360
TVLDYDKIGK NDAIGKVFVG YNSTGAELRH WSDMLANPRR PIAQWHTLQV EEEVDAMLAV 420
KK 422 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
 GO:0060201; C:clathrin-sculpted acetylcholine transport vesicle membrane; TAS:Reactome.
 GO:0061202; C:clathrin-sculpted gamma-aminobutyric acid transport vesicle membrane; TAS:Reactome.
 GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
 GO:0070083; C:clathrin-sculpted monoamine transport vesicle membrane; TAS:Reactome.
 GO:0031045; C:dense core granule; IEA:Compara.
 GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
 GO:0060076; C:excitatory synapse; IEA:Compara.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0042734; C:presynaptic membrane; IEA:Compara.
 GO:0008021; C:synaptic vesicle; TAS:UniProtKB.
 GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0005545; F:1-phosphatidylinositol binding; TAS:UniProtKB.
 GO:0005509; F:calcium ion binding; IEA:Compara.
 GO:0005544; F:calcium-dependent phospholipid binding; IEA:Compara.
 GO:0050750; F:low-density lipoprotein particle receptor binding; IDA:MGI.
 GO:0017075; F:syntaxin-1 binding; TAS:UniProtKB.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0005513; P:detection of calcium ion; TAS:UniProtKB.
 GO:0014047; P:glutamate secretion; TAS:Reactome.
 GO:0007269; P:neurotransmitter secretion; TAS:UniProtKB.
 GO:0051260; P:protein homooligomerization; TAS:UniProtKB.
 GO:0017158; P:regulation of calcium ion-dependent exocytosis; IEA:Compara.
 GO:0017157; P:regulation of exocytosis; TAS:UniProtKB.
 GO:0016079; P:synaptic vesicle exocytosis; IEA:Compara. 
Interpro
 IPR000008; C2_Ca-dep.
 IPR008973; C2_Ca/lipid-bd_dom_CaLB.
 IPR020477; C2_dom.
 IPR018029; C2_membr_targeting.
 IPR001565; Synaptotagmin.
 IPR015428; Synaptotagmin1. 
Pfam
 PF00168; C2 
SMART
 SM00239; C2 
PROSITE
 PS50004; C2 
PRINTS
 PR00360; C2DOMAIN.
 PR00399; SYNAPTOTAGMN.