Eps8
entrez
312812
canonical
uniprot
F1M3L7
canonical
ensembl
ENSRNOG00000007047
resolver
ensp
ENSRNOP00000009328
resolver
genesymbol
Eps8
resolver
uniprot_entry
EPS8_RAT
resolver
amino_acid_sequence
MNGHMSNHSSGYGIYPSQMNGYGSSPPYSQMDREHCSRTSAKALYEQRKNYARDSVSSVSDVSQYRVEHLTTFVLDRKDAMITVDDGIRKLKLLDAKGKVWTQDMILQVDDRAVSLIDLESKNELENFPLNTIQHCQAVAHTCSYDSILALVCKEPTQNKPDLHLFQCDEVKANLISEDIESAISDSKGGKQKRRPEALRMIAKADPGIPPPPRAPAPVPPGTVTQVDVRSRVAAWSAWAADQGDFEKPRQYHEQEETPEMMAARIDRDVQILNHILDDIEFFITKLQKAAEAFSELSKRKKSKKSKRKGPGEGVLTLRAKPPPPDEFVDCFQKFKHGFNLLAKLKSHIQNPSASDLVHFLFTPLNMVVQATGGPELASSVLSPLLTKDTVDFLNYTVKAEERQLWMSLGETWMKVRAEWPKEQFIPPYVPRFRNGWEPPMLNFMGAPTEQDMYQLAESVANAAEQQRKQDSKRQSTEHSSMSDYPPADGYTFSNSMYHRGPHVDQGEAALALKSTPNRHVDRNYDPVKTQPKKYAKSKYDFVARNSSELSVMKDDVLEILDDRKQWWKVRNASGDSGFVPNNILDIMRTPESGVGRTDPPYTHTIQKQRTEYGPRSADTPSAPSPPPTPAPVPVPLPPSAPAPVPVPKVPANVTRQNSSSSESGGSIARDSQRYKQLPVDRRKSQMEEVQDELFQRLTIGRSAAQRKFHVPRQNVPVINITYDSSPEEVKTWLQSKGFNPVTVSSLGVLNGAQLFSLNKDELRSVCPEGARVFSQITVQKAALEDSSGSSELQEIMRRRQEKISAAASDSGVESFDEGSSH
uniprot
proteins
function
FUNCTION: Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with WHRN and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes (By similarity). {ECO:0000250}.
uniprot
proteins
mass_dalton
91929
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated by the SCF(FBXW5) E3 ubiquitin-protein ligase complex during G2 phase, leading to its transient degradation and subsequent cell shape changes required to allow mitotic progression. Reappears at the midzone of dividing cells (By similarity). {ECO:0000250}.; PTM: Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation. Phosphorylated by several receptor tyrosine kinases (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
EPS8 family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16641100
uniprot
proteins
pubmed
17304222
uniprot
proteins
pubmed
19564905
uniprot
proteins
pubmed
22673903
uniprot
proteins
sequence_length
822
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Synapse, synaptosome. Cytoplasm, cell cortex {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Cell projection, stereocilium {ECO:0000250, ECO:0000250|UniProtKB:Q08509}. Cell projection, growth cone. Note=Localizes at the tips of the stereocilia of the inner and outer hair cells (By similarity). Localizes to the midzone of dividing cells. {ECO:0000250, ECO:0000250|UniProtKB:Q08509}.
uniprot
proteins