Protein detail

EPS8

Epidermal growth factor receptor kinase substrate 8

Entry name
EPS8
UniProt ID
EVMP confidence score
0.72
Supporting publications (n)
11
Transmembrane count
Protein classification
Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
EVMP confidence score

Annotation confidence score; open for threshold definitions.

Extremely high >= 0.85High >= 0.70Medium >= 0.55Low >= 0.40
Basic Information10
Protein Names
Epidermal growth factor receptor kinase substrate 8
Protein Class (4)
Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function (3)
  • Disease related genes
  • Predicted intracellular proteins
  • Human disease related genes:Nervous system diseases:Ear disease
Entrez Gene Symbol
Gene Description
Epidermal growth factor receptor pathway substrate 8
Chromosome
12
Position
15620134-15882329
Supporting publications (n)
11
EVMP confidence score
0.72
Fluorescence & Localization1
EPS8 fluorescence
Function & Pathway6
Relations & Evidence27

Enzyme-Mediated Modification (8)

8 records.

Substrate Gene SymbolEnzyme Gene SymbolEnzyme UniProt IDResidue TypeResidue OffsetModificationDatabaseReferences
EPS8PTK6Q13882Y535phosphorylationSIGNORSIGNOR:28214294
EPS8PTK6Q13882Y498phosphorylationREACH_ProtMapperSIGNORProtMapperProtMapper:28214294SIGNOR:27738316
EPS8PTK6Q13882Y525phosphorylationREACH_ProtMapperSIGNORProtMapperProtMapper:28214294SIGNOR:28214294
EPS8MAPK3P27361S625phosphorylationSIGNORSIGNOR:19564905
EPS8SRCP12931Y485phosphorylationPhosphoSite
EPS8SRCP12931Y774phosphorylationPhosphoSite
EPS8SRCP12931Y525phosphorylationPhosphoSite
EPS8SRCP12931Y602phosphorylationPhosphoSite

Ligand-Receptor Signaling (5)

5 records.

CategoryParentDatabaseTransmitterReceiverSecretedPlasma Membrane (Transmembrane)Plasma Membrane (Peripheral)
intracellularintracellularLOCATENoNoNoNoNo
intracellularintracellularComPPINoNoNoNoNo
intracellularintracellularGO_IntercellNoNoNoNoNo
intracellularintracellularUniProt_locationNoNoNoNoNo
intracellularintracellularOmniPathNoNoNoNoNo

Regulatory Interaction Network (3)

3 records.

Source Protein SymbolSource UniProt IDTarget Protein SymbolTarget UniProt IDIs DirectedIs StimulationIs InhibitionDatabaseReferences
MK03P27361EPS8Q12929YesNoYesSIGNOR_ProtMapperiPTMnetSIGNORProtMapperSIGNOR:19564905ProtMapper:19564905
PTK6Q13882EPS8Q12929YesYesNoiPTMnetSIGNORProtMapperSIGNOR_ProtMapperREACH_ProtMapperProtMapper:28214294SIGNOR:27738316ProtMapper:27738316SIGNOR:28214294
SRCP12931EPS8Q12929YesYesNoWangPhosphoSite_norefPhosphoPointProtMapperHPRDCui2007SPIKE_LCPhosphoSitePhosphoSite_ProtMapperSPIKE_LC:16189514HPRD:10395945PhosphoSite:32641864PhosphoSite:23626693

Protein Complex Composition (10)

10 records.

Component NameComponent Gene SymbolsComponent UniProt IDStoichiometryDatabaseDatabase IDsReferences
EIF1BEIF3BEIF3DEIF3FEIF3GEIF3HEIF3JEIF3KEIF3LEIF3MEIF4A2EPS8TP53RKO00303O15371O15372O60739O75821O75822P55884Q12929Q14240Q7L2H7Q96S44Q9UBQ5Q9Y2621:1:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC8343
CMC1CTBP2EPS8L2HNRNPH3LRRC47TAX1BP3O14907P31942P56545Q7Z7K0Q8N1G4Q9H6S30:0:0:0:0:0hu.MAP2
CARM1CIMIP4CMC1CPNE3EPS8L2HNRNPH1O43247O75131P31943Q7Z7K0Q86X55Q9H6S30:0:0:0:0:0hu.MAP2
BLOC1S2BLOC1S6CCDC22DTNBP1EPS8H4C4SMARCD1SNAPINO60826O95295P62805Q12929Q6QNY1Q96EV8Q96GM5Q9UL451:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC9305
BLOC1S2BLOC1S6EPS8NAT10SMARCD1SNAPINO95295Q12929Q6QNY1Q96GM5Q9H0A0Q9UL451:1:1:1:1:1NetworkBlastCompleatCompleat:HC6570
BAG6EPS8GET4RAC1TRNAU1APUBCP0CG48P46379P63000Q12929Q7L5D6Q9NX071:1:1:1:1:1NetworkBlastCompleatCompleat:HC7987
EPS8TAF10TAF11TAF12TAF2TAF3TAF4BTAF5TAF6TAF8TBPYBX1P20226P49848P67809Q12929Q12962Q15542Q15544Q16514Q5VWG9Q6P1X5Q7Z7C8Q927501:1:1:1:1:1:1:1:1:1:1:1NetworkBlastCompleatCompleat:HC6452
AMPD2EPS8Q01433Q129290:0hu.MAP2
EPS8TOMM34Q12929Q157850:0hu.MAP
CMC1EPS8L2Q7Z7K0Q9H6S30:0hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation MethodDetection MethodNumber of ReferencesReferences
Differential UltracentrifugationMass spectrometry127821849
Sequence, Structure & Domains14

Sequences

Length
822
Mass
91,882
Sequence
MNGHISNHPSSFGMYPSQMNGYGSSPTFSQTDREHGSKTSAKALYEQRKNYARDSVSSVSDISQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVMHSCSYDSVLALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPDALRMISNADPSIPPPPRAPAPAPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKNKKGKRKGPGEGVLTLRAKPPPPDEFLDCFQKFKHGFNLLAKLKSHIQNPSAADLVHFLFTPLNMVVQATGGPELASSVLSPLLNKDTIDFLNYTVNGDERQLWMSLGGTWMKARAEWPKEQFIPPYVPRFRNGWEPPMLNFMGATMEQDLYQLAESVANVAEHQRKQEIKRLSTEHSSVSEYHPADGYAFSSNIYTRGSHLDQGEAAVAFKPTSNRHIDRNYEPLKTQPKKYAKSKYDFVARNNSELSVLKDDILEILDDRKQWWKVRNASGDSGFVPNNILDIVRPPESGLGRADPPYTHTIQKQRMEYGPRPADTPPAPSPPPTPAPVPVPLPPSTPAPVPVSKVPANITRQNSSSSDSGGSIVRDSQRHKQLPVDRRKSQMEEVQDELIHRLTIGRSAAQKKFHVPRQNVPVINITYDSTPEDVKTWLQSKGFNPVTVNSLGVLNGAQLFSLNKDELRTVCPEGARVYSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH
Alternative Products
Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q12929-1; Sequence=Displayed; Name=2; IsoId=Q12929-2; Sequence=VSP_056460
Alternative Sequence
1..260; Missing (in isoform 2)

3D Structural Models

Helix
582..584; 729..737; 741..746; 752..757; 760..766; 770..784
Beta Strand
535..540; 557..562; 564..571; 577..581; 585..587; 748..750
3D Structure
NMR spectroscopy (1); X-ray crystallography (1)

Domain & Motif Annotations

Compositional Bias
1..10; Polar residues; 17..30; Polar residues; 208..221; Pro residues; 299..309; Basic residues; 618..645; Pro residues; 671..687; Basic and acidic residues
Domain (CC)
The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. It mediates both barbed-end actin capping and actin bundling activities. The capping activity is mediated by an amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers, while the bundling activity is mediated by a compact 4 helix bundle, which contacts 3 actin subunits along the filament (By similarity).; DOMAIN: The SH3 domain mediates interaction with SHB.
Domain (FT)
64..194; PTB; 531..590; SH3
Region
1..39; Disordered; 202..225; Disordered; 298..320; Disordered; 612..689; Disordered; 649..822; Effector region; 680..698; Amphipathic helix; 718..738; Helix bundle 1; 752..757; Helix bundle 2; 762..767; Helix bundle 3; 766..785; Helix bundle 4; 787..822; Disordered
Protein Families
EPS8 family
Sequence Similarities
Belongs to the EPS8 family.
Clinical Relevance6
Disease Involvement (2)
DeafnessNon-syndromic deafness
Interaction Protein (5)
ENSG00000006453ENSG00000110395ENSG00000146648ENSG00000164904ENSG00000175866
Interaction Count
5
Interaction Dataset
intact_biogrid
Supporting Publications11
PMIDTitleAbstract
34265469Proteomic Landscape of Exosomes Reveals the Functional Contributions of CD151 in Triple-Negative Breast Cancer.Furthermore, utilizing quantitative proteomics approach to reveal the proteomes of CD151-deleted exosomes and cells, we found that exosomal CD151 facilitated secretion of ribosomal proteins via exosomes while inhibiting exosome secretion of complement proteins. Moreover, we proved that CD151-deleted exosomes significantly decreased the migration and invasion of TNBC cells. Most importantly, we found that the tetraspanin CD151 expression levels in TNBC-derived serum exosomes were significantly higher than those exosomes from healthy subjects, and we validated our findings with samples from 16 additional donors. This is the first comparative study of the proteomes of TNBC patient-derived and CD151-deleted exosomes.
36507906Proteomics Analysis of Plasma-Derived Exosomes Unveils the Aberrant Complement and Coagulation Cascades in Dermatomyositis/Polymyositis.No abstract available
36573687Proteomic and phosphoproteomic landscape of salivary extracellular vesicles to assess OSCC therapeutical outcomes.No abstract available
38037300Proteomic profiling of paired human liver homogenate and tissue derived extracellular vesicles.No abstract available
38576002Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation.No abstract available
39773168TGF-β Receptor-dependent Tissue Factor Release and Proteomic Profiling of Extracellular Vesicles from Mechanically Compressed Human Bronchial Epithelial Cells.No abstract available
39948040Quantitative proteomics identifies possible flow of metastatic cues between progressive stages of colorectal cancer via transfer of ceramide-dependent exosomal cargoes.No abstract available
39996590Surface Double Dendritic Magnetic Microfibrils for Rapid Isolation and Proteomic Profiling of Extracellular Vesicles from Microliters of Biofluids.No abstract available
40596376Proteomic profiling of plasma extracellular vesicles identifies signatures of innate immunity, coagulation, and endothelial activation in septic patients.No abstract available
40689422Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.No abstract available
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