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Epidermal growth factor receptor kinase substrate 8

 EPS8_MOUSE              Reviewed;         821 AA.
Q08509; Q3TM41;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
22-NOV-2017, entry version 163.
RecName: Full=Epidermal growth factor receptor kinase substrate 8;
Name=Eps8;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN CELL GROWTH, INTERACTION WITH
EGFR, AND PHOSPHORYLATION.
PubMed=8404850;
Fazioli F., Minichiello L., Matoska V., Castagnino P., Miki T.,
Wong W.T., di Fiore P.P.;
"Eps8, a substrate for the epidermal growth factor receptor kinase,
enhances EGF-dependent mitogenic signals.";
EMBO J. 12:3799-3808(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Bone marrow, and Lung;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Kidney;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
INTERACTION WITH SHB.
PubMed=7537362;
Karlsson T., Songyang Z., Landgren E., Lavergne C., Di Fiore P.P.,
Anafi M., Pawson T., Cantley L.C., Claesson-Welsh L., Welsh M.;
"Molecular interactions of the Src homology 2 domain protein Shb with
phosphotyrosine residues, tyrosine kinase receptors and Src homology 3
domain proteins.";
Oncogene 10:1475-1483(1995).
[5]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH ABI1 AND SOS1, AND
DISRUPTION PHENOTYPE.
PubMed=10499589; DOI=10.1038/45822;
Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S.,
Bjarnegard M., Betsholtz C., Di Fiore P.P.;
"EPS8 and E3B1 transduce signals from Ras to Rac.";
Nature 401:290-293(1999).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SOS1.
PubMed=11524436; DOI=10.1083/jcb.200103146;
Scita G., Tenca P., Areces L.B., Tocchetti A., Frittoli E.,
Giardina G., Ponzanelli I., Sini P., Innocenti M., Di Fiore P.P.;
"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.";
J. Cell Biol. 154:1031-1044(2001).
[7]
REVIEW ON FUNCTION.
PubMed=12127568; DOI=10.1016/S1357-2725(02)00064-X;
Di Fiore P.P., Scita G.;
"Eps8 in the midst of GTPases.";
Int. J. Biochem. Cell Biol. 34:1178-1183(2002).
[8]
FUNCTION, AND INTERACTION WITH ABI1.
PubMed=15558031; DOI=10.1038/ncb1199;
Disanza A., Carlier M.F., Stradal T.E., Didry D., Frittoli E.,
Confalonieri S., Croce A., Wehland J., Di Fiore P.P., Scita G.;
"Eps8 controls actin-based motility by capping the barbed ends of
actin filaments.";
Nat. Cell Biol. 6:1180-1188(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=15592455; DOI=10.1038/nbt1046;
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.;
"Immunoaffinity profiling of tyrosine phosphorylation in cancer
cells.";
Nat. Biotechnol. 23:94-101(2005).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain;
PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,
Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic
density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[11]
FUNCTION, AND INTERACTION WITH BAIAP2.
PubMed=17115031; DOI=10.1038/ncb1502;
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.;
"Regulation of cell shape by Cdc42 is mediated by the synergic actin-
bundling activity of the Eps8-IRSp53 complex.";
Nat. Cell Biol. 8:1337-1347(2006).
[12]
INTERACTION WITH LANCL1.
PubMed=19528316; DOI=10.1101/gad.1789209;
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.;
"Structure of human lanthionine synthetase C-like protein 1 and its
interaction with Eps8 and glutathione.";
Genes Dev. 23:1387-1392(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-658, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[14]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION AT SER-624 AND THR-628,
AND MUTAGENESIS OF SER-624 AND THR-628.
PubMed=19564905; DOI=10.1371/journal.pbio.1000138;
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.;
"Eps8 regulates axonal filopodia in hippocampal neurons in response to
brain-derived neurotrophic factor (BDNF).";
PLoS Biol. 7:E1000138-E1000138(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-658; SER-661;
SER-684; SER-810 AND SER-814, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, and Lung;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[16]
FUNCTION, AND MUTAGENESIS OF VAL-689; LEU-693; ARG-706 AND PHE-708.
PubMed=20532239; DOI=10.1371/journal.pbio.1000387;
Hertzog M., Milanesi F., Hazelwood L., Disanza A., Liu H., Perlade E.,
Malabarba M.G., Pasqualato S., Maiolica A., Confalonieri S.,
Le Clainche C., Offenhauser N., Block J., Rottner K., Di Fiore P.P.,
Carlier M.F., Volkmann N., Hanein D., Scita G.;
"Molecular basis for the dual function of Eps8 on actin dynamics:
bundling and capping.";
PLoS Biol. 8:E1000387-E1000387(2010).
[17]
FUNCTION, INTERACTION WITH MYO15A AND WHRN, SUBCELLULAR LOCATION, AND
DISRUPTION PHENOTYPE.
PubMed=21236676; DOI=10.1016/j.cub.2010.12.046;
Manor U., Disanza A., Grati M., Andrade L., Lin H., Di Fiore P.P.,
Scita G., Kachar B.;
"Regulation of stereocilia length by myosin XVa and whirlin depends on
the actin-regulatory protein Eps8.";
Curr. Biol. 21:167-172(2011).
[18]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=21835647; DOI=10.1016/j.immuni.2011.07.007;
Frittoli E., Matteoli G., Palamidessi A., Mazzini E., Maddaluno L.,
Disanza A., Yang C., Svitkina T., Rescigno M., Scita G.;
"The signaling adaptor Eps8 is an essential actin capping protein for
dendritic cell migration.";
Immunity 35:388-399(2011).
[19]
SUBCELLULAR LOCATION, AND UBIQUITINATION.
PubMed=23314863; DOI=10.1038/ncb2661;
Werner A., Disanza A., Reifenberger N., Habeck G., Becker J.,
Calabrese M., Urlaub H., Lorenz H., Schulman B., Scita G.,
Melchior F.;
"SCF(Fbxw5) mediates transient degradation of actin remodeller Eps8 to
allow proper mitotic progression.";
Nat. Cell Biol. 15:179-188(2013).
[20]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=23918390; DOI=10.1073/pnas.1304644110;
Furness D.N., Johnson S.L., Manor U., Ruettiger L., Tocchetti A.,
Offenhauser N., Olt J., Goodyear R.J., Vijayakumar S., Dai Y.,
Hackney C.M., Franz C., Di Fiore P.P., Masetto S., Jones S.M.,
Knipper M., Holley M.C., Richardson G.P., Kachar B., Marcotti W.;
"Progressive hearing loss and gradual deterioration of sensory hair
bundles in the ears of mice lacking the actin-binding protein
Eps8L2.";
Proc. Natl. Acad. Sci. U.S.A. 110:13898-13903(2013).
[21]
SUBCELLULAR LOCATION.
PubMed=24741995; DOI=10.1186/1750-1172-9-55;
Behlouli A., Bonnet C., Abdi S., Bouaita A., Lelli A., Hardelin J.P.,
Schietroma C., Rous Y., Louha M., Cheknane A., Lebdi H.,
Boudjelida K., Makrelouf M., Zenati A., Petit C.;
"EPS8, encoding an actin-binding protein of cochlear hair cell
stereocilia, is a new causal gene for autosomal recessive profound
deafness.";
Orphanet J. Rare Dis. 9:55-55(2014).
[22]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 532-591, AND
HOMODIMERIZATION.
PubMed=9303002; DOI=10.1038/nsb0997-739;
Kishan K.V.R., Scita G., Wong W.T., di Fiore P.P., Newcomer M.E.;
"The SH3 domain of Eps8 exists as a novel intertwined dimer.";
Nat. Struct. Biol. 4:739-743(1997).
-!- 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. {ECO:0000269|PubMed:10499589,
ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:15558031,
ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19564905,
ECO:0000269|PubMed:20532239, ECO:0000269|PubMed:21236676,
ECO:0000269|PubMed:21835647, ECO:0000269|PubMed:8404850}.
-!- SUBUNIT: 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 WHRN. {ECO:0000269|PubMed:10499589,
ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:15558031,
ECO:0000269|PubMed:17115031, ECO:0000269|PubMed:19528316,
ECO:0000269|PubMed:21236676, ECO:0000269|PubMed:7537362,
ECO:0000269|PubMed:8404850}.
-!- INTERACTION:
Q8IZP0:ABI1 (xeno); NbExp=2; IntAct=EBI-375596, EBI-375446;
Q8CBW3:Abi1; NbExp=3; IntAct=EBI-375596, EBI-375511;
Q9UQB8:BAIAP2 (xeno); NbExp=8; IntAct=EBI-375596, EBI-525456;
O43813:LANCL1 (xeno); NbExp=2; IntAct=EBI-375596, EBI-3046631;
P27361:MAPK3 (xeno); NbExp=2; IntAct=EBI-375596, EBI-73995;
-!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Cell projection,
ruffle membrane. Cell projection, growth cone {ECO:0000250}. Cell
projection, stereocilium {ECO:0000269|PubMed:23918390,
ECO:0000269|PubMed:24741995}. Cell junction, synapse, synaptosome
{ECO:0000250}. Note=Localizes at the tips of the stereocilia of
the inner and outer hair cells (PubMed:24741995, PubMed:23918390).
Localizes to the midzone of dividing cells.
{ECO:0000269|PubMed:23918390, ECO:0000269|PubMed:24741995}.
-!- TISSUE SPECIFICITY: Expressed in neuronal cell body and neurites,
and prominently enriched in the axonal growth cone
(PubMed:19564905). Expressed at the tips of cochlear hair cells
stereocilia (PubMed:23918390). {ECO:0000269|PubMed:19564905,
ECO:0000269|PubMed:23918390}.
-!- DOMAIN: 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).
{ECO:0000269|PubMed:11524436, ECO:0000269|PubMed:20532239}.
-!- DOMAIN: The SH3 domain mediates interaction with SHB.
{ECO:0000250}.
-!- 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.
{ECO:0000269|PubMed:23314863}.
-!- PTM: 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.
{ECO:0000269|PubMed:19564905, ECO:0000269|PubMed:8404850}.
-!- DISRUPTION PHENOTYPE: 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.
{ECO:0000269|PubMed:10499589, ECO:0000269|PubMed:21236676,
ECO:0000269|PubMed:21835647}.
-!- SIMILARITY: Belongs to the EPS8 family. {ECO:0000305}.
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EMBL; L21671; AAA16358.1; -; mRNA.
EMBL; AK149683; BAE29023.1; -; mRNA.
EMBL; AK166156; BAE38601.1; -; mRNA.
EMBL; BC016890; AAH16890.1; -; mRNA.
CCDS; CCDS20665.1; -.
PIR; S39983; S39983.
RefSeq; NP_001258516.1; NM_001271587.1.
RefSeq; NP_001258517.1; NM_001271588.1.
RefSeq; NP_001258518.1; NM_001271589.1.
RefSeq; NP_001258524.1; NM_001271595.1.
RefSeq; NP_031971.2; NM_007945.3.
RefSeq; XP_011239506.1; XM_011241204.2.
UniGene; Mm.235346; -.
UniGene; Mm.412332; -.
PDB; 1AOJ; X-ray; 2.50 A; A/B=532-591.
PDB; 1I07; X-ray; 1.80 A; A/B=532-591.
PDB; 1I0C; X-ray; 2.00 A; A/B=532-591.
PDBsum; 1AOJ; -.
PDBsum; 1I07; -.
PDBsum; 1I0C; -.
ProteinModelPortal; Q08509; -.
SMR; Q08509; -.
BioGrid; 199491; 8.
CORUM; Q08509; -.
DIP; DIP-32858N; -.
IntAct; Q08509; 11.
MINT; MINT-1506131; -.
STRING; 10090.ENSMUSP00000052776; -.
iPTMnet; Q08509; -.
PhosphoSitePlus; Q08509; -.
EPD; Q08509; -.
MaxQB; Q08509; -.
PaxDb; Q08509; -.
PeptideAtlas; Q08509; -.
PRIDE; Q08509; -.
Ensembl; ENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766.
Ensembl; ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766.
Ensembl; ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766.
GeneID; 13860; -.
KEGG; mmu:13860; -.
UCSC; uc009emz.2; mouse.
CTD; 2059; -.
MGI; MGI:104684; Eps8.
eggNOG; KOG3557; Eukaryota.
eggNOG; ENOG410XT9R; LUCA.
GeneTree; ENSGT00390000003646; -.
HOGENOM; HOG000060324; -.
HOVERGEN; HBG003090; -.
InParanoid; Q08509; -.
KO; K17277; -.
OMA; AEWPKEQ; -.
OrthoDB; EOG091G023T; -.
TreeFam; TF313069; -.
EvolutionaryTrace; Q08509; -.
PRO; PR:Q08509; -.
Proteomes; UP000000589; Chromosome 6.
Bgee; ENSMUSG00000015766; -.
ExpressionAtlas; Q08509; baseline and differential.
Genevisible; Q08509; MM.
GO; GO:0005903; C:brush border; IDA:UniProtKB.
GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
GO; GO:0017146; C:NMDA selective glutamate receptor complex; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0032587; C:ruffle membrane; IDA:UniProtKB.
GO; GO:0032420; C:stereocilium; IDA:UniProtKB.
GO; GO:0045202; C:synapse; IDA:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0003779; F:actin binding; IDA:UniProtKB.
GO; GO:0048365; F:Rac GTPase binding; IDA:UniProtKB.
GO; GO:0035591; F:signaling adaptor activity; IEA:InterPro.
GO; GO:0051764; P:actin crosslink formation; IDA:UniProtKB.
GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
GO; GO:0070358; P:actin polymerization-dependent cell motility; IDA:UniProtKB.
GO; GO:0008344; P:adult locomotory behavior; IMP:MGI.
GO; GO:0051016; P:barbed-end actin filament capping; IDA:UniProtKB.
GO; GO:0048149; P:behavioral response to ethanol; IMP:MGI.
GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
GO; GO:0036336; P:dendritic cell migration; IMP:UniProtKB.
GO; GO:0010458; P:exit from mitosis; IMP:UniProtKB.
GO; GO:0016601; P:Rac protein signal transduction; IDA:UniProtKB.
GO; GO:0030832; P:regulation of actin filament length; IMP:UniProtKB.
GO; GO:0008360; P:regulation of cell shape; IMP:UniProtKB.
CDD; cd01210; PTB_EPS8; 1.
CDD; cd11764; SH3_Eps8; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR030222; EPS8.
InterPro; IPR033928; EPS8_PTB.
InterPro; IPR035462; Eps8_SH3.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR013625; PTB.
InterPro; IPR006020; PTB/PI_dom.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
PANTHER; PTHR12287:SF21; PTHR12287:SF21; 1.
Pfam; PF08416; PTB; 1.
Pfam; PF00018; SH3_1; 1.
SMART; SM00462; PTB; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell junction; Cell membrane;
Cell projection; Complete proteome; Cytoplasm; Membrane;
Phosphoprotein; Reference proteome; SH3 domain; Synapse; Synaptosome;
Ubl conjugation.
CHAIN 1 821 Epidermal growth factor receptor kinase
substrate 8.
/FTId=PRO_0000086995.
DOMAIN 69 129 PH; first part.
DOMAIN 381 414 PH; second part.
DOMAIN 530 589 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REGION 648 821 Effector region.
REGION 679 697 Amphipathic helix.
REGION 717 737 Helix bundle 1.
REGION 751 756 Helix bundle 2.
REGION 761 766 Helix bundle 3.
REGION 765 784 Helix bundle 4.
COMPBIAS 210 213 Poly-Pro.
COMPBIAS 322 325 Poly-Pro.
COMPBIAS 421 440 Pro-rich.
COMPBIAS 620 650 Pro-rich.
COMPBIAS 658 663 Poly-Ser.
MOD_RES 58 58 Phosphoserine.
{ECO:0000250|UniProtKB:F1M3L7}.
MOD_RES 223 223 Phosphothreonine.
{ECO:0000250|UniProtKB:Q12929}.
MOD_RES 317 317 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 475 475 Phosphoserine.
{ECO:0000250|UniProtKB:Q12929}.
MOD_RES 624 624 Phosphoserine; by MAPK.
{ECO:0000269|PubMed:19564905}.
MOD_RES 628 628 Phosphothreonine; by MAPK.
{ECO:0000269|PubMed:19564905}.
MOD_RES 658 658 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 810 810 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 814 814 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MUTAGEN 624 624 S->A: Does not detach from actin
following BDNF treatment; when associated
with A-628.
{ECO:0000269|PubMed:19564905}.
MUTAGEN 624 624 S->E: Mimicks phosphorylation state;
promotes detachment from actin in absence
of BDNF treatment; when associated with
E-628. {ECO:0000269|PubMed:19564905}.
MUTAGEN 628 628 T->A: Does not detach from actin
following BDNF treatment; when associated
with A-624.
{ECO:0000269|PubMed:19564905}.
MUTAGEN 628 628 T->E: Mimicks phosphorylation state;
promotes detachment from actin in absence
of BDNF treatment; when associated with
E-624. {ECO:0000269|PubMed:19564905}.
MUTAGEN 689 689 V->D: Abolishes barbed-end actin-binding
without affecting actin bundling
activity. {ECO:0000269|PubMed:20532239}.
MUTAGEN 693 693 L->D: Abolishes barbed-end actin-binding
without affecting actin bundling
activity. {ECO:0000269|PubMed:20532239}.
MUTAGEN 706 706 R->A: Impairs both actin capping and
bundling activities.
{ECO:0000269|PubMed:20532239}.
MUTAGEN 708 708 F->A: Impairs both actin capping and
bundling activities.
{ECO:0000269|PubMed:20532239}.
CONFLICT 652 652 N -> D (in Ref. 1; AAA16358 and 3;
AAH16890). {ECO:0000305}.
STRAND 534 539 {ECO:0000244|PDB:1I07}.
STRAND 556 559 {ECO:0000244|PDB:1I07}.
HELIX 561 563 {ECO:0000244|PDB:1I07}.
STRAND 566 570 {ECO:0000244|PDB:1I07}.
STRAND 576 580 {ECO:0000244|PDB:1I07}.
HELIX 581 583 {ECO:0000244|PDB:1I07}.
STRAND 584 587 {ECO:0000244|PDB:1I07}.
SEQUENCE 821 AA; 91737 MW; 50F691FAC3EF1304 CRC64;
MNGHMSNRSS GYGVYPSQLN GYGSSPPYSQ MDREHSSRTS AKALYEQRKN YARDSVSSVS
DVSQYRVEHL TTFVLDRKDA MITVEDGIRK LKLLDAKGKV WTQDMILQVD DRAVSLIDLE
SKNELENFPL NTISHCQAVV HACSYDSILA LVCKEPTQSK PDLHLFQCDE VKANLISEDI
ESAISDSKGG KQKRRPEALR MIAKADPGIP PPPRAPAPVP PGTVTQVDVR SRVAAWSAWA
ADQGDFEKPR QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR
KKSKKSKRKG PGEGVLTLRA KPPPPDEFVD CFQKFKHGFN LLAKLKSHIQ NPSASDLVHF
LFTPLNMVVQ ATGGPELASS VLSPLLTKDT VDFLNYTATA EERKLWMSLG DSWVKVRAEW
PKEQFIPPYV PRFRNGWEPP MLNFMGAPTE QDMYQLAESV ANAEHQRKQD SKRLSTEHSN
VSDYPPADGY AYSSSMYHRG PHADHGEAAM PFKSTPNHQV DRNYDAVKTQ PKKYAKSKYD
FVARNSSELS VMKDDVLEIL DDRRQWWKVR NASGDSGFVP NNILDIMRTP ESGVGRADPP
YTHTIQKQRT EYGLRSADTP SAPSPPPTPA PVPVPLPPSV PAPVSVPKVP ANVTRQNSSS
SDSGGSIVRD SQRYKQLPVD RRKSQMEEVQ DELFQRLTIG RSAAQRKFHV PRQNVPVINI
TYDSSPEEVK TWLQSKGFNP VTVNSLGVLN GAQLFSLNKD ELRSVCPEGA RVFNQITVQK
AALEDSNGSS ELQEIMRRRQ EKISAAASDS GVESFDEGSS H


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