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Q08509

- EPS8_MOUSE

UniProt

Q08509 - EPS8_MOUSE

Protein

Epidermal growth factor receptor kinase substrate 8

Gene

Eps8

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    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 DFNB31 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.9 Publications

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. Rac GTPase binding Source: UniProtKB

    GO - Biological processi

    1. actin crosslink formation Source: UniProtKB
    2. actin cytoskeleton reorganization Source: MGI
    3. actin filament bundle assembly Source: UniProtKB
    4. actin polymerization-dependent cell motility Source: UniProtKB
    5. adult locomotory behavior Source: MGI
    6. barbed-end actin filament capping Source: UniProtKB
    7. behavioral response to ethanol Source: MGI
    8. dendritic cell migration Source: UniProtKB
    9. exit from mitosis Source: UniProtKB
    10. Rac protein signal transduction Source: UniProtKB
    11. regulation of actin filament length Source: UniProtKB
    12. regulation of cell shape Source: UniProtKB

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epidermal growth factor receptor kinase substrate 8
    Gene namesi
    Name:Eps8
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:104684. Eps8.

    Subcellular locationi

    Cytoplasmcell cortex. Cell projectionruffle membrane. Cell projectiongrowth cone By similarity. Cell projectionstereocilium. Cell junctionsynapsesynaptosome By similarity
    Note: Localizes to the midzone of dividing cells.

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. cell junction Source: UniProtKB-KW
    3. extracellular vesicular exosome Source: Ensembl
    4. growth cone Source: UniProtKB-SubCell
    5. N-methyl-D-aspartate selective glutamate receptor complex Source: MGI
    6. postsynaptic density Source: MGI
    7. ruffle membrane Source: UniProtKB
    8. stereocilium Source: UniProtKB
    9. synapse Source: MGI

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Defects in PDGF-induced membrane ruffling due to defects in Ras to Rac signals. Dendritic cells are impaired in directional and chemotactic migration and are delayed in reaching the draining lymph node in vivo after inflammatory challenge. Mice show short stereocilia.3 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi624 – 6241S → A: Does not detach from actin following BDNF treatment; when associated with A-628. 1 Publication
    Mutagenesisi624 – 6241S → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-628. 1 Publication
    Mutagenesisi628 – 6281T → A: Does not detach from actin following BDNF treatment; when associated with A-624. 1 Publication
    Mutagenesisi628 – 6281T → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-624. 1 Publication
    Mutagenesisi689 – 6891V → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. 1 Publication
    Mutagenesisi693 – 6931L → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. 1 Publication
    Mutagenesisi706 – 7061R → A: Impairs both actin capping and bundling activities. 1 Publication
    Mutagenesisi708 – 7081F → A: Impairs both actin capping and bundling activities. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 821821Epidermal growth factor receptor kinase substrate 8PRO_0000086995Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei317 – 3171PhosphothreonineBy similarity
    Modified residuei475 – 4751PhosphoserineBy similarity
    Modified residuei624 – 6241Phosphoserine; by MAPK2 Publications
    Modified residuei628 – 6281Phosphothreonine; by MAPK2 Publications
    Modified residuei658 – 6581Phosphoserine2 Publications

    Post-translational modificationi

    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.1 Publication
    Phosphorylation at Ser-624 and Thr-628 by MAPK following BDNF treatment promotes removal from actin and filopodia formation. Phosphorylated by several receptor tyrosine kinases.3 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ08509.
    PaxDbiQ08509.
    PRIDEiQ08509.

    PTM databases

    PhosphoSiteiQ08509.

    Expressioni

    Tissue specificityi

    Expressed in neuronal cell body and neurites, and prominently enriched in the axonal growth cone.1 Publication

    Gene expression databases

    ArrayExpressiQ08509.
    BgeeiQ08509.
    GenevestigatoriQ08509.

    Interactioni

    Subunit structurei

    Homodimer. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with BAIAP2. Interacts with SHB and LANCL1. Interacts with EGFR; mediates EPS8 phosphorylation. Interacts with MYO15A and DFNB31.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ABI1Q8IZP02EBI-375596,EBI-375446From a different organism.
    Abi1Q8CBW32EBI-375596,EBI-375511
    BAIAP2Q9UQB88EBI-375596,EBI-525456From a different organism.
    LANCL1O438132EBI-375596,EBI-3046631From a different organism.

    Protein-protein interaction databases

    BioGridi199491. 5 interactions.
    DIPiDIP-32858N.
    IntActiQ08509. 7 interactions.
    MINTiMINT-1506131.

    Structurei

    Secondary structure

    1
    821
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi534 – 5396
    Beta strandi556 – 5594
    Helixi561 – 5633
    Beta strandi566 – 5705
    Beta strandi576 – 5805
    Helixi581 – 5833
    Beta strandi584 – 5874

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1AOJX-ray2.50A/B532-591[»]
    1I07X-ray1.80A/B532-591[»]
    1I0CX-ray2.00A/B532-591[»]
    ProteinModelPortaliQ08509.
    SMRiQ08509. Positions 59-188, 532-590, 698-783.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ08509.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 12961PH; first partAdd
    BLAST
    Domaini381 – 41434PH; second partAdd
    BLAST
    Domaini532 – 59160SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni648 – 821174Effector regionAdd
    BLAST
    Regioni679 – 69719Amphipathic helixAdd
    BLAST
    Regioni717 – 73721Helix bundle 1Add
    BLAST
    Regioni751 – 7566Helix bundle 2
    Regioni761 – 7666Helix bundle 3
    Regioni765 – 78420Helix bundle 4Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi210 – 2134Poly-Pro
    Compositional biasi322 – 3254Poly-Pro
    Compositional biasi421 – 44020Pro-richAdd
    BLAST
    Compositional biasi620 – 65031Pro-richAdd
    BLAST
    Compositional biasi658 – 6636Poly-Ser

    Domaini

    The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity (PubMed:11524436). It mediates both barbed-end actin capping and actin bundling activities (PubMed:20532239). 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 (PubMed:20532239).2 Publications
    The SH3 domain mediates interaction with SHB.By similarity

    Sequence similaritiesi

    Belongs to the EPS8 family.Curated
    Contains 1 PH domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    SH3 domain

    Phylogenomic databases

    eggNOGiNOG263108.
    GeneTreeiENSGT00390000003646.
    HOGENOMiHOG000060324.
    HOVERGENiHBG003090.
    InParanoidiQ3TM41.
    KOiK17277.
    OMAiIPPYVPR.
    OrthoDBiEOG7TMZR9.
    TreeFamiTF313069.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR013625. PTB.
    IPR006020. PTB/PI_dom.
    IPR001452. SH3_domain.
    [Graphical view]
    PfamiPF08416. PTB. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view]
    SMARTiSM00462. PTB. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view]
    SUPFAMiSSF50044. SSF50044. 1 hit.
    PROSITEiPS50002. SH3. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q08509-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNGHMSNRSS GYGVYPSQLN GYGSSPPYSQ MDREHSSRTS AKALYEQRKN    50
    YARDSVSSVS DVSQYRVEHL TTFVLDRKDA MITVEDGIRK LKLLDAKGKV 100
    WTQDMILQVD DRAVSLIDLE SKNELENFPL NTISHCQAVV HACSYDSILA 150
    LVCKEPTQSK PDLHLFQCDE VKANLISEDI ESAISDSKGG KQKRRPEALR 200
    MIAKADPGIP PPPRAPAPVP PGTVTQVDVR SRVAAWSAWA ADQGDFEKPR 250
    QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR 300
    KKSKKSKRKG PGEGVLTLRA KPPPPDEFVD CFQKFKHGFN LLAKLKSHIQ 350
    NPSASDLVHF LFTPLNMVVQ ATGGPELASS VLSPLLTKDT VDFLNYTATA 400
    EERKLWMSLG DSWVKVRAEW PKEQFIPPYV PRFRNGWEPP MLNFMGAPTE 450
    QDMYQLAESV ANAEHQRKQD SKRLSTEHSN VSDYPPADGY AYSSSMYHRG 500
    PHADHGEAAM PFKSTPNHQV DRNYDAVKTQ PKKYAKSKYD FVARNSSELS 550
    VMKDDVLEIL DDRRQWWKVR NASGDSGFVP NNILDIMRTP ESGVGRADPP 600
    YTHTIQKQRT EYGLRSADTP SAPSPPPTPA PVPVPLPPSV PAPVSVPKVP 650
    ANVTRQNSSS SDSGGSIVRD SQRYKQLPVD RRKSQMEEVQ DELFQRLTIG 700
    RSAAQRKFHV PRQNVPVINI TYDSSPEEVK TWLQSKGFNP VTVNSLGVLN 750
    GAQLFSLNKD ELRSVCPEGA RVFNQITVQK AALEDSNGSS ELQEIMRRRQ 800
    EKISAAASDS GVESFDEGSS H 821
    Length:821
    Mass (Da):91,737
    Last modified:July 27, 2011 - v2
    Checksum:i50F691FAC3EF1304
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti652 – 6521N → D in AAA16358. (PubMed:8404850)Curated
    Sequence conflicti652 – 6521N → D in AAH16890. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21671 mRNA. Translation: AAA16358.1.
    AK149683 mRNA. Translation: BAE29023.1.
    AK166156 mRNA. Translation: BAE38601.1.
    BC016890 mRNA. Translation: AAH16890.1.
    CCDSiCCDS20665.1.
    PIRiS39983.
    RefSeqiNP_001258516.1. NM_001271587.1.
    NP_001258517.1. NM_001271588.1.
    NP_001258518.1. NM_001271589.1.
    NP_001258524.1. NM_001271595.1.
    NP_031971.2. NM_007945.3.
    XP_006505570.1. XM_006505507.1.
    UniGeneiMm.235346.
    Mm.412332.

    Genome annotation databases

    EnsembliENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766.
    ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766.
    ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766.
    GeneIDi13860.
    KEGGimmu:13860.
    UCSCiuc009emz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L21671 mRNA. Translation: AAA16358.1 .
    AK149683 mRNA. Translation: BAE29023.1 .
    AK166156 mRNA. Translation: BAE38601.1 .
    BC016890 mRNA. Translation: AAH16890.1 .
    CCDSi CCDS20665.1.
    PIRi S39983.
    RefSeqi NP_001258516.1. NM_001271587.1.
    NP_001258517.1. NM_001271588.1.
    NP_001258518.1. NM_001271589.1.
    NP_001258524.1. NM_001271595.1.
    NP_031971.2. NM_007945.3.
    XP_006505570.1. XM_006505507.1.
    UniGenei Mm.235346.
    Mm.412332.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1AOJ X-ray 2.50 A/B 532-591 [» ]
    1I07 X-ray 1.80 A/B 532-591 [» ]
    1I0C X-ray 2.00 A/B 532-591 [» ]
    ProteinModelPortali Q08509.
    SMRi Q08509. Positions 59-188, 532-590, 698-783.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199491. 5 interactions.
    DIPi DIP-32858N.
    IntActi Q08509. 7 interactions.
    MINTi MINT-1506131.

    PTM databases

    PhosphoSitei Q08509.

    Proteomic databases

    MaxQBi Q08509.
    PaxDbi Q08509.
    PRIDEi Q08509.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058210 ; ENSMUSP00000052776 ; ENSMUSG00000015766 .
    ENSMUST00000100841 ; ENSMUSP00000098402 ; ENSMUSG00000015766 .
    ENSMUST00000111878 ; ENSMUSP00000107509 ; ENSMUSG00000015766 .
    GeneIDi 13860.
    KEGGi mmu:13860.
    UCSCi uc009emz.1. mouse.

    Organism-specific databases

    CTDi 2059.
    MGIi MGI:104684. Eps8.

    Phylogenomic databases

    eggNOGi NOG263108.
    GeneTreei ENSGT00390000003646.
    HOGENOMi HOG000060324.
    HOVERGENi HBG003090.
    InParanoidi Q3TM41.
    KOi K17277.
    OMAi IPPYVPR.
    OrthoDBi EOG7TMZR9.
    TreeFami TF313069.

    Miscellaneous databases

    ChiTaRSi EPS8. mouse.
    EvolutionaryTracei Q08509.
    NextBioi 284742.
    PROi Q08509.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q08509.
    Bgeei Q08509.
    Genevestigatori Q08509.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR013625. PTB.
    IPR006020. PTB/PI_dom.
    IPR001452. SH3_domain.
    [Graphical view ]
    Pfami PF08416. PTB. 1 hit.
    PF00018. SH3_1. 1 hit.
    [Graphical view ]
    SMARTi SM00462. PTB. 1 hit.
    SM00326. SH3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50044. SSF50044. 1 hit.
    PROSITEi PS50002. SH3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals."
      Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T., Wong W.T., di Fiore P.P.
      EMBO J. 12:3799-3808(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CELL GROWTH, INTERACTION WITH EGFR, PHOSPHORYLATION.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Bone marrow and Lung.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Kidney.
    4. "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins."
      Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P., Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.
      Oncogene 10:1475-1483(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SHB.
    5. Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, DISRUPTION PHENOTYPE.
    6. "An effector region in Eps8 is responsible for the activation of the Rac-specific GEF activity of Sos-1 and for the proper localization of the Rac-based actin-polymerizing machine."
      Scita G., Tenca P., Areces L.B., Tocchetti A., Frittoli E., Giardina G., Ponzanelli I., Sini P., Innocenti M., Di Fiore P.P.
      J. Cell Biol. 154:1031-1044(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SOS1.
    7. Cited for: REVIEW ON FUNCTION.
    8. "Eps8 controls actin-based motility by capping the barbed ends of actin filaments."
      Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E., Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.
      Nat. Cell Biol. 6:1180-1188(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ABI1.
    9. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
      Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
      Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    11. "Regulation of cell shape by Cdc42 is mediated by the synergic actin-bundling activity of the Eps8-IRSp53 complex."
      Disanza A., Mantoani S., Hertzog M., Gerboth S., Frittoli E., Steffen A., Berhoerster K., Kreienkamp H.J., Milanesi F., Di Fiore P.P., Ciliberto A., Stradal T.E., Scita G.
      Nat. Cell Biol. 8:1337-1347(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BAIAP2.
    12. "Structure of human lanthionine synthetase C-like protein 1 and its interaction with Eps8 and glutathione."
      Zhang W., Wang L., Liu Y., Xu J., Zhu G., Cang H., Li X., Bartlam M., Hensley K., Li G., Rao Z., Zhang X.C.
      Genes Dev. 23:1387-1392(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LANCL1.
    13. "The phagosomal proteome in interferon-gamma-activated macrophages."
      Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
      Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Eps8 regulates axonal filopodia in hippocampal neurons in response to brain-derived neurotrophic factor (BDNF)."
      Menna E., Disanza A., Cagnoli C., Schenk U., Gelsomino G., Frittoli E., Hertzog M., Offenhauser N., Sawallisch C., Kreienkamp H.J., Gertler F.B., Di Fiore P.P., Scita G., Matteoli M.
      PLoS Biol. 7:E1000138-E1000138(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-624 AND THR-628, MUTAGENESIS OF SER-624 AND THR-628.
    15. Cited for: FUNCTION, MUTAGENESIS OF VAL-689; LEU-693; ARG-706 AND PHE-708.
    16. "Regulation of stereocilia length by myosin XVa and whirlin depends on the actin-regulatory protein Eps8."
      Manor U., Disanza A., Grati M., Andrade L., Lin H., Di Fiore P.P., Scita G., Kachar B.
      Curr. Biol. 21:167-172(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH MYO15A AND DFNB31, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    17. "The signaling adaptor Eps8 is an essential actin capping protein for dendritic cell migration."
      Frittoli E., Matteoli G., Palamidessi A., Mazzini E., Maddaluno L., Disanza A., Yang C., Svitkina T., Rescigno M., Scita G.
      Immunity 35:388-399(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    18. "SCF(Fbxw5) mediates transient degradation of actin remodeller Eps8 to allow proper mitotic progression."
      Werner A., Disanza A., Reifenberger N., Habeck G., Becker J., Calabrese M., Urlaub H., Lorenz H., Schulman B., Scita G., Melchior F.
      Nat. Cell Biol. 15:179-188(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, UBIQUITINATION.
    19. "The SH3 domain of Eps8 exists as a novel intertwined dimer."
      Kishan K.V.R., Scita G., Wong W.T., di Fiore P.P., Newcomer M.E.
      Nat. Struct. Biol. 4:739-743(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 532-591, HOMODIMERIZATION.

    Entry informationi

    Entry nameiEPS8_MOUSE
    AccessioniPrimary (citable) accession number: Q08509
    Secondary accession number(s): Q3TM41
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3