Protein detail

EPS8

Epidermal growth factor receptor kinase substrate 8

Protein symbol
EPS8
UniProt ID
EVMP score
0.72
Frequency
11
Transmembrane count
Protein classification
Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Basic Information
Protein Names
Epidermal growth factor receptor kinase substrate 8
Protein Class
Disease related genesHuman disease related genesPlasma proteinsPredicted intracellular proteins
Protein Function
  • 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
Frequency
11
EVMP Score
0.72
Fluorescence & Localization
Function & Pathway
Relations & Evidence

Enzyme-Mediated Modification

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 records.

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

Regulatory Interaction Network

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

Isolation & Detection Technology

1 record.

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

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 Relevance
Disease Involvement
DeafnessNon-syndromic deafness
Interaction Protein
ENSG00000006453ENSG00000110395ENSG00000146648ENSG00000164904ENSG00000175866
Interaction Count
5
Interaction Dataset
intact_biogrid