Protein detail
ESYT2
Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)
Protein symbol ESYT2 | UniProt ID | EVMP score 0.72 |
Frequency 19 | Transmembrane count 2 | Protein classification Plasma proteinsPredicted membrane proteinsTransporters |
Basic Information
Protein Names
Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)
Protein Class
Plasma proteinsPredicted membrane proteinsTransporters
Protein Function
Transporters
Transmembrane
104..124; Helical; 128..148; Helical
Transmembrane Count
2
Ensembl
Entrez Gene Symbol
Gene Synonym
CHR2SYTFAM62BKIAA1228
Gene Description
Extended synaptotagmin 2
Chromosome
7
Position
158730995-158830253
Frequency
19
EVMP Score
0.72
Fluorescence & Localization
Tissue Specificheart muscleCell SpecificAdipocytesBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway
Protein Function
Transporters
Cellular Component
Molecular Function
Biological Process
Mediation Categories
Fusion and delivery mediation
Relations & Evidence
Enzyme-Mediated Modification
0 records.
Ligand-Receptor Signaling
15 records.
| Category | Parent | Database | Transmitter | Receiver | Secreted | Plasma Membrane (Transmembrane) | Plasma Membrane (Peripheral) |
|---|---|---|---|---|---|---|---|
| intracellular | intracellular | ComPPI | No | No | No | No | No |
| intracellular | intracellular | GO_Intercell | No | No | No | No | No |
| intracellular | intracellular | UniProt_location | No | No | No | No | No |
| intracellular | intracellular | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_location | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_topology | No | No | No | No | No |
| transmembrane | transmembrane | UniProt_keyword | No | No | No | No | No |
| transmembrane_predicted | transmembrane | OmniPath | No | No | No | No | No |
| transmembrane | transmembrane | TopDB | No | No | No | No | No |
| transmembrane | transmembrane | Ramilowski_location | No | No | No | No | No |
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Regulatory Interaction Network
0 records.
Protein Complex Composition
Sequence, Structure & Domains
Sequences
Length
921
Mass
102,357
Sequence
MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGGPENPGGVLSVELPGLLAQLARSFALLLPVYALGYLGLSFSWVLLALALLAWCRRSRGLKALRLCRALALLEDEERVVRLGVRACDLPAWVHFPDTERAEWLNKTVKHMWPFICQFIEKLFRETIEPAVRGANTHLSTFSFTKVDVGQQPLRINGVKVYTENVDKRQIILDLQISFVGNCEIDLEIKRYFCRAGVKSIQIHGTMRVILEPLIGDMPLVGALSIFFLRKPLLEINWTGLTNLLDVPGLNGLSDTIILDIISNYLVLPNRITVPLVSEVQIAQLRFPVPKGVLRIHFIEAQDLQGKDTYLKGLVKGKSDPYGIIRVGNQIFQSRVIKENLSPKWNEVYEALVYEHPGQELEIELFDEDPDKDDFLGSLMIDLIEVEKERLLDEWFTLDEVPKGKLHLRLEWLTLMPNASNLDKVLTDIKADKDQANDGLSSALLILYLDSARNLPSGKKISSNPNPVVQMSVGHKAQESKIRYKTNEPVWEENFTFFIHNPKRQDLEVEVRDEQHQCSLGNLKVPLSQLLTSEDMTVSQRFQLSNSGPNSTIKMKIALRVLHLEKRERPPDHQHSAQVKRPSVSKEGRKTSIKSHMSGSPGPGGSNTAPSTPVIGGSDKPGMEEKAQPPEAGPQGLHDLGRSSSSLLASPGHISVKEPTPSIASDISLPIATQELRQRLRQLENGTTLGQSPLGQIQLTIRHSSQRNKLIVVVHACRNLIAFSEDGSDPYVRMYLLPDKRRSGRRKTHVSKKTLNPVFDQSFDFSVSLPEVQRRTLDVAVKNSGGFLSKDKGLLGKVLVALASEELAKGWTQWYDLTEDGTRPQAMT
Alternative Products
Event=Alternative splicing; Named isoforms=5; Name=1; IsoId=A0FGR8-1; Sequence=Displayed; Name=2; IsoId=A0FGR8-2; Sequence=VSP_023239; Name=4; IsoId=A0FGR8-4; Sequence=VSP_023238, VSP_023241, VSP_023242; Name=5; IsoId=A0FGR8-5; Sequence=VSP_023236, VSP_023240; Name=6; IsoId=A0FGR8-6; Sequence=VSP_038324
Alternative Sequence
1..593; Missing (in isoform 5); 1..204; Missing (in isoform 4); 1..97; MTANRDAALSSHRHPGCAQRPRTPTFASSSQRRSAFGFDDGNFPGLGERSHAPGSRLGARRRAKTARGLRGHRQRGAGAGLSRPGSARAPSPPRPGG -> MTPPSRAEAGVRRSRVPSEGRWRGAEPPGISASTQPASAGRAARHCGAMSGARGEGPEAGAGGAGGRAA (in isoform 2); 550; S -> SNPLEFNPDVLKKTAVQRALKS (in isoform 6); 594..603; NPKRQDLEVE -> MPVLPPCVLQ (in isoform 5); 706..731; PVIGGSDKPGMEEKAQPPEAGPQGLH -> SQSRSRPPASPRTSRCPSPPRSCGKG (in isoform 4); 732..921; Missing (in isoform 4)
3D Structural Models
Turn
283..286; 341..345; 405..407; 595..597; 607..609; 798..801; 899..902
Helix
196..219; 221..226; 230..232; 334..337; 348..358; 372..379; 476..482; 515..524; 621..624; 627..629; 862..867
Beta Strand
235..241; 248..255; 264..282; 287..304; 316..323; 326..333; 365..370; 384..396; 414..420; 423..426; 437..446; 453..460; 463..465; 467..475; 483..490; 494..496; 498..512; 535..547; 552..554; 560..566; 569..572; 583..593; 599..606; 612..619; 630..636; 638..640; 645..656; 789..797; 802..811; 823..831; 835..837; 851..858; 869..876; 889..894
3D Structure
NMR spectroscopy (1); X-ray crystallography (3)
Domain & Motif Annotations
Compositional Bias
58..75; Basic residues
Domain (CC)
Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.; DOMAIN: The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium (PubMed:24373768). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane (PubMed:23791178).; DOMAIN: The SMP-LTD domain is a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (PubMed:24847877).
Domain (FT)
191..370; SMP-LTD; 369..489; C2 1; 514..639; C2 2; 786..908; C2 3
Region
1..103; Disordered; 660..754; Disordered; 833..840; Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane
Protein Families
Extended synaptotagmin family
Sequence Similarities
Belongs to the extended synaptotagmin family.
Clinical Relevance
Interaction Protein
ENSG00000101558ENSG00000124164ENSG00000139641ENSG00000170027
Interaction Count
4
Interaction Dataset
biogrid_opencellintact_biogrid_opencell