Protein detail

EPS8

Epidermal growth factor receptor kinase substrate 8

Entry name EPS8	UniProt ID Q12929	EVMP confidence score 0.72
Supporting publications (n) 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 (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

Ensembl

ENSG00000151491

Entrez Gene Symbol

EPS8

Gene Description

Epidermal growth factor receptor pathway substrate 8

Chromosome

Position

15620134-15882329

Supporting publications (n)

EVMP confidence score

0.72

Fluorescence & Localization

Function & Pathway

Protein Function (3)

Disease related genes
Predicted intracellular proteins
Human disease related genes:Nervous system diseases:Ear disease

Cellular Component (12)

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Molecular Function (3)

Biological Process (3)

Reactome (3)

Mediation Categories (3)

Fusion and delivery mediationImmune mediationReceptor-signaling mediation

Relations & Evidence27

Enzyme-Mediated Modification (8)

8 records.

Substrate Gene Symbol	Enzyme Gene Symbol	Enzyme UniProt ID	Residue Type	Residue Offset	Modification	Database	References
EPS8	PTK6	Q13882	Y	535	phosphorylation	SIGNOR	SIGNOR:28214294
EPS8	PTK6	Q13882	Y	498	phosphorylation	REACH_ProtMapperSIGNORProtMapper	ProtMapper:28214294 SIGNOR:27738316
EPS8	PTK6	Q13882	Y	525	phosphorylation	REACH_ProtMapperSIGNORProtMapper	ProtMapper:28214294 SIGNOR:28214294
EPS8	MAPK3	P27361	S	625	phosphorylation	SIGNOR	SIGNOR:19564905
EPS8	SRC	P12931	Y	485	phosphorylation	PhosphoSite
EPS8	SRC	P12931	Y	774	phosphorylation	PhosphoSite
EPS8	SRC	P12931	Y	525	phosphorylation	PhosphoSite
EPS8	SRC	P12931	Y	602	phosphorylation	PhosphoSite

Ligand-Receptor Signaling (5)

5 records.

Category	Parent	Database
intracellular	intracellular	LOCATE
intracellular	intracellular	ComPPI
intracellular	intracellular	GO_Intercell
intracellular	intracellular	UniProt_location
intracellular	intracellular	OmniPath

Regulatory Interaction Network (3)

3 records.

Source Protein Symbol	Source UniProt ID	Target Protein Symbol	Target UniProt ID	Is Directed	Is Stimulation	Is Inhibition	Database	References
MK03	P27361	EPS8	Q12929	Yes		Yes	SIGNOR_ProtMapperiPTMnetSIGNORProtMapper	SIGNOR:19564905 ProtMapper:19564905
PTK6	Q13882	EPS8	Q12929	Yes	Yes		iPTMnetSIGNORProtMapperSIGNOR_ProtMapperREACH_ProtMapper	ProtMapper:28214294 SIGNOR:27738316 ProtMapper:27738316 SIGNOR:28214294
SRC	P12931	EPS8	Q12929	Yes	Yes		WangPhosphoSite_norefPhosphoPointProtMapperHPRDCui2007SPIKE_LCPhosphoSitePhosphoSite_ProtMapper	SPIKE_LC:16189514 HPRD:10395945 PhosphoSite:32641864 PhosphoSite:23626693

Protein Complex Composition (10)

10 records.

Component Gene Symbols	Component UniProt ID	Stoichiometry	Database	Database IDs
EIF1B EIF3B EIF3D EIF3F EIF3G EIF3H EIF3J EIF3K EIF3L EIF3M EIF4A2 EPS8 TP53RK	O00303 O15371 O15372 O60739 O75821 O75822 P55884 Q12929 Q14240 Q7L2H7 Q96S44 Q9UBQ5 Q9Y262	1:1:1:1:1:1:1:1:1:1:1:1:1	NetworkBlastCompleat	Compleat:HC8343
CMC1 CTBP2 EPS8L2 HNRNPH3 LRRC47 TAX1BP3	O14907 P31942 P56545 Q7Z7K0 Q8N1G4 Q9H6S3	0:0:0:0:0:0	hu.MAP2
CARM1 CIMIP4 CMC1 CPNE3 EPS8L2 HNRNPH1	O43247 O75131 P31943 Q7Z7K0 Q86X55 Q9H6S3	0:0:0:0:0:0	hu.MAP2
BLOC1S2 BLOC1S6 CCDC22 DTNBP1 EPS8 H4C4 SMARCD1 SNAPIN	O60826 O95295 P62805 Q12929 Q6QNY1 Q96EV8 Q96GM5 Q9UL45	1:1:1:1:1:1:1:1	NetworkBlastCompleat	Compleat:HC9305
BLOC1S2 BLOC1S6 EPS8 NAT10 SMARCD1 SNAPIN	O95295 Q12929 Q6QNY1 Q96GM5 Q9H0A0 Q9UL45	1:1:1:1:1:1	NetworkBlastCompleat	Compleat:HC6570
BAG6 EPS8 GET4 RAC1 TRNAU1AP UBC	P0CG48 P46379 P63000 Q12929 Q7L5D6 Q9NX07	1:1:1:1:1:1	NetworkBlastCompleat	Compleat:HC7987
EPS8 TAF10 TAF11 TAF12 TAF2 TAF3 TAF4B TAF5 TAF6 TAF8 TBP YBX1	P20226 P49848 P67809 Q12929 Q12962 Q15542 Q15544 Q16514 Q5VWG9 Q6P1X5 Q7Z7C8 Q92750	1:1:1:1:1:1:1:1:1:1:1:1	NetworkBlastCompleat	Compleat:HC6452
AMPD2 EPS8	Q01433 Q12929	0:0	hu.MAP2
EPS8 TOMM34	Q12929 Q15785	0:0	hu.MAP
CMC1 EPS8L2	Q7Z7K0 Q9H6S3	0:0	hu.MAP2

Isolation & Detection Technology (1)

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential Ultracentrifugation	Mass spectrometry	1	27821849

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 (2)

DeafnessNon-syndromic deafness

Related Diseases (2)

Deafness Non-syndromic deafness

Antibody (2)

HPA003897 HPA050209

Interaction Protein (5)

ENSG00000006453ENSG00000110395ENSG00000146648ENSG00000164904ENSG00000175866

Interaction Count

Interaction Dataset

intact_biogrid

Supporting Publications11

PMID	Title	Related sentences
34265469	Proteomic 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.
36507906	Proteomics Analysis of Plasma-Derived Exosomes Unveils the Aberrant Complement and Coagulation Cascades in Dermatomyositis/Polymyositis.	No related sentences available
36573687	Proteomic and phosphoproteomic landscape of salivary extracellular vesicles to assess OSCC therapeutical outcomes.	No related sentences available
38037300	Proteomic profiling of paired human liver homogenate and tissue derived extracellular vesicles.	No related sentences available
38576002	Therapy-induced senescent tumor cell-derived extracellular vesicles promote colorectal cancer progression through SERPINE1-mediated NF-κB p65 nuclear translocation.	No related sentences available
39773168	TGF-β Receptor-dependent Tissue Factor Release and Proteomic Profiling of Extracellular Vesicles from Mechanically Compressed Human Bronchial Epithelial Cells.	No related sentences available
39948040	Quantitative proteomics identifies possible flow of metastatic cues between progressive stages of colorectal cancer via transfer of ceramide-dependent exosomal cargoes.	No related sentences available
39996590	Surface Double Dendritic Magnetic Microfibrils for Rapid Isolation and Proteomic Profiling of Extracellular Vesicles from Microliters of Biofluids.	No related sentences available
40596376	Proteomic profiling of plasma extracellular vesicles identifies signatures of innate immunity, coagulation, and endothelial activation in septic patients.	No related sentences available
40689422	Defining the Ovarian Cancer Precancerous Landscape through Modeling Fallopian Tube Epithelium Reprogramming Driven by Extracellular Vesicles.	No related sentences available

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