Protein detail

ESYT2

Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)

Entry name
ESYT2
UniProt ID
EVMP confidence score
0.72
Supporting publications (n)
19
Transmembrane count
2
Protein classification
Plasma proteinsPredicted membrane proteinsTransporters
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information13
Protein Names
Extended synaptotagmin-2 (E-Syt2) (Chr2Syt)
Protein Class (3)
Plasma proteinsPredicted membrane proteinsTransporters
Protein Function
Transporters
Transmembrane
104..124; Helical; 128..148; Helical
Transmembrane Count
2
Entrez Gene Symbol
Gene Synonym (3)
CHR2SYTFAM62BKIAA1228
Gene Description
Extended synaptotagmin 2
Chromosome
7
Position
158730995-158830253
Supporting publications (n)
19
EVMP confidence score
0.72
Fluorescence & Localization5
ESYT2 fluorescence
Tissue Specificheart muscleCell SpecificAdipocytesBlood Cell SpecificneutrophilBlood Lineage Specificgranulocytes
Function & Pathway6
Relations & Evidence19

Ligand-Receptor Signaling (15)

15 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
transmembranetransmembraneOmniPathNoNoNoNoNo
plasma_membraneplasma_membraneUniProt_locationNoNoNoNoNo
plasma_membraneplasma_membraneOmniPathNoNoNoNoNo
transmembranetransmembrane_predictedPhobiusNoNoNoNoNo
transmembrane_tmhmmtransmembrane_predictedAlmen2009NoNoNoNoNo
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Protein Complex Composition (3)

3 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
ESYT1-ESYT2 complexESYT1ESYT2A0FGR8Q9BSJ80:0CORUMCORUM:731323791178
ESYT2A0FGR82PDBPDB:4p42PDB:4npj
COX15ESYT2A0FGR8Q7KZN90:0hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationSize Exclusion ChromatographyMass spectrometry22782184938716512
Sequence, Structure & Domains15

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 Relevance5
Interaction Protein (4)
ENSG00000101558ENSG00000124164ENSG00000139641ENSG00000170027
Interaction Count
4
Interaction Dataset (2)
biogrid_opencellintact_biogrid_opencell
Supporting Publications18
PMIDTitleAbstract
36398564Differential ultracentrifugation enables deep plasma proteomics through enrichment of extracellular vesicles.No abstract available
37786918Rapid and in-depth proteomic profiling of small extracellular vesicles for ultralow samples.No abstract available
38168906Defining the relationship between cellular and extracellular vesicle (EV) content in breast cancer via an integrative multi-omic analysis.No abstract available
38321535Identification of specific markers for human pluripotent stem cell-derived small extracellular vesicles.No abstract available
39569406Proteomics of circulating extracellular vesicles reveals diverse clinical presentations of COVID-19 but fails to identify viral peptides.No abstract available
39766158A Proteomic Examination of Plasma Extracellular Vesicles Across Colorectal Cancer Stages Uncovers Biological Insights That Potentially Improve Prognosis.No abstract available
40748658Exosomes released from senescent cells and circulatory exosomes isolated from human plasma reveal aging-associated proteomic and lipid signatures.No abstract available
41216884Extracellular Vesicles From Multiple Sclerosis White Matter Exhibit Synaptic, Mitochondrial, Complement and Ageing-Related Pathway Dysregulation.No abstract available
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