CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-004996
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
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
98KGKEKGGKNAINMKDacetylation[1]
98KGKEKGGKNAINMKDubiquitination[2]
104GKNAINMKDVKDLGKubiquitination[2]
119TMKDQALKDDDAETGubiquitination[2]
190VFLLPDKKKKFETKVubiquitination[2]
200FETKVHRKTLNPVFNubiquitination[2]
213FNEQFTFKVPYSELGacetylation[1]
236YDFDRFSKHDIIGEFubiquitination[2]
267RDLQSAEKEEQEKLGacetylation[1]
267RDLQSAEKEEQEKLGubiquitination[2]
297TVVILEAKNLKKMDVubiquitination[2]
369LDYDKIGKNDAIGKVubiquitination[2]
375GKNDAIGKVFVGYNSubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113] 
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 143 244 C2 1.
 DOMAIN 274 377 C2 2.
 REGION 135 381 Phospholipid binding (Probable).
 METAL 171 171 Calcium 2; via carbonyl oxygen.
 METAL 172 172 Calcium 1.
 METAL 172 172 Calcium 2.
 METAL 178 178 Calcium 1.
 METAL 230 230 Calcium 1.
 METAL 230 230 Calcium 2.
 METAL 231 231 Calcium 1; via carbonyl oxygen.
 METAL 232 232 Calcium 1.
 METAL 232 232 Calcium 2.
 METAL 232 232 Calcium 3.
 METAL 235 235 Calcium 3.
 METAL 236 236 Calcium 3; via carbonyl oxygen.
 METAL 238 238 Calcium 2.
 METAL 238 238 Calcium 3.
 MOD_RES 128 128 Phosphothreonine (By similarity).
 MOD_RES 229 229 Phosphotyrosine (By similarity).
 MOD_RES 364 364 Phosphotyrosine (By similarity).
 MOD_RES 380 380 Phosphotyrosine (By similarity).
 LIPID 74 74 S-palmitoyl cysteine.
 LIPID 75 75 S-palmitoyl cysteine.
 LIPID 77 77 S-palmitoyl cysteine.
 LIPID 79 79 S-palmitoyl cysteine.
 LIPID 82 82 S-palmitoyl cysteine.
 CARBOHYD 24 24 N-linked (GlcNAc...).  
Keyword
 3D-structure; Calcium; Cell junction; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing; Glycoprotein; Lipoprotein; Membrane; Metal-binding; Palmitate; Phosphoprotein; Reference proteome; Repeat; Synapse; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 421 AA 
Protein Sequence
MVSASHPEAL AAPVTTVATL VPHNATEPAS PGEGKEDAFS KLKQKFMNEL HKIPLPPWAL 60
IAIAIVAVLL VVTCCFCVCK KCLFKKKNKK KGKEKGGKNA INMKDVKDLG KTMKDQALKD 120
DDAETGLTDG EEKEEPKEEE KLGKLQYSLD YDFQNNQLLV GIIQAAELPA LDMGGTSDPY 180
VKVFLLPDKK KKFETKVHRK TLNPVFNEQF TFKVPYSELG GKTLVMAVYD FDRFSKHDII 240
GEFKVPMNTV DFGHVTEEWR DLQSAEKEEQ EKLGDICFSL RYVPTAGKLT VVILEAKNLK 300
KMDVGGLSDP YVKIHLMQNG KRLKKKKTTI KKNTLNPYYN ESFSFEVPFE QIQKVQVVVT 360
VLDYDKIGKN DAIGKVFVGY NSTGAELRHW SDMLANPRRP IAQWHTLQVE EEVDAMLAVK 420
K 421 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0042584; C:chromaffin granule membrane; IEA:UniProtKB-SubCell.
 GO:0031045; C:dense core granule; IDA:MGI.
 GO:0060076; C:excitatory synapse; IDA:BHF-UCL.
 GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
 GO:0043005; C:neuron projection; IEA:Compara.
 GO:0005886; C:plasma membrane; IDA:BHF-UCL.
 GO:0042734; C:presynaptic membrane; IEA:Compara.
 GO:0030672; C:synaptic vesicle membrane; TAS:RGD.
 GO:0005509; F:calcium ion binding; IDA:RGD.
 GO:0005544; F:calcium-dependent phospholipid binding; IDA:BHF-UCL.
 GO:0048306; F:calcium-dependent protein binding; IDA:RGD.
 GO:0005516; F:calmodulin binding; IDA:RGD.
 GO:0030276; F:clathrin binding; IDA:BHF-UCL.
 GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:RGD.
 GO:0001786; F:phosphatidylserine binding; IDA:RGD.
 GO:0017075; F:syntaxin-1 binding; IDA:RGD.
 GO:0005215; F:transporter activity; IEA:InterPro.
 GO:0017156; P:calcium ion-dependent exocytosis; TAS:RGD.
 GO:0005513; P:detection of calcium ion; IDA:RGD.
 GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:RGD.
 GO:0031340; P:positive regulation of vesicle fusion; IDA:RGD.
 GO:0016079; P:synaptic vesicle exocytosis; TAS:RGD.
 GO:0048278; P:vesicle docking; IDA:RGD. 
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.