SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q08509

- EPS8_MOUSE

UniProt

Q08509 - EPS8_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

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

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

GO - Biological processi

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

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.3 Publications

GO - Cellular componenti

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

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 8
PRO_0000086995Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171Phosphothreonine By similarity
Modified residuei475 – 4751Phosphoserine By similarity
Modified residuei624 – 6241Phosphoserine; by MAPK1 Publication
Modified residuei628 – 6281Phosphothreonine; by MAPK1 Publication
Modified residuei658 – 6581Phosphoserine1 Publication

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.2 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 DFNB31.9 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

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.

Miscellaneous databases

EvolutionaryTraceiQ08509.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 12961PH; first part
Add
BLAST
Domaini381 – 41434PH; second part
Add
BLAST
Domaini532 – 59160SH3
Add
BLAST

Region

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

Compositional bias

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

Domaini

The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity (1 Publication). It mediates both barbed-end actin capping and actin bundling activities (1 Publication). 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 (1 Publication).
The SH3 domain mediates interaction with SHB By similarity.

Sequence similaritiesi

Belongs to the EPS8 family.
Contains 1 PH domain.
Contains 1 SH3 domain.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti652 – 6521N → D in AAA16358. 1 Publication
Sequence conflicti652 – 6521N → D in AAH16890. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 133 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

Similar proteinsi