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Q08509 (EPS8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor kinase substrate 8
Gene names
Name:Eps8
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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 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. Ref.1 Ref.5 Ref.6 Ref.8 Ref.11 Ref.14 Ref.15 Ref.16 Ref.17

Subunit structure

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. Ref.1 Ref.4 Ref.5 Ref.6 Ref.8 Ref.11 Ref.12 Ref.16 Ref.19

Subcellular location

Cytoplasmcell cortex. Cell projectionruffle membrane. Cell projectiongrowth cone By similarity. Cell projectionstereocilium. Cell junctionsynapsesynaptosome By similarity. Note: Localizes to the midzone of dividing cells. Ref.6 Ref.16 Ref.18

Tissue specificity

Expressed in neuronal cell body and neurites, and prominently enriched in the axonal growth cone. Ref.14

Domain

The effector region is required for activating the Rac-specific guanine nucleotide exchange factor (GEF) activity (Ref.6). It mediates both barbed-end actin capping and actin bundling activities (Ref.15). 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 (Ref.15).

The SH3 domain mediates interaction with SHB By similarity.

Post-translational modification

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. Ref.18

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. Ref.1 Ref.14

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. Ref.5 Ref.16 Ref.17

Sequence similarities

Belongs to the EPS8 family.

Contains 1 PH domain.

Contains 1 SH3 domain.

Ontologies

Keywords
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
Synapse
Synaptosome
   DomainSH3 domain
   LigandActin-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from direct assay Ref.6. Source: UniProtKB

actin crosslink formation

Inferred from direct assay Ref.15. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from mutant phenotype PubMed 17018287. Source: MGI

actin filament bundle assembly

Inferred from direct assay Ref.15. Source: UniProtKB

actin polymerization-dependent cell motility

Inferred from direct assay Ref.8. Source: UniProtKB

adult locomotory behavior

Inferred from mutant phenotype PubMed 17018287. Source: MGI

barbed-end actin filament capping

Inferred from direct assay Ref.8Ref.15. Source: UniProtKB

behavioral response to ethanol

Inferred from mutant phenotype PubMed 17018287. Source: MGI

dendritic cell migration

Inferred from mutant phenotype Ref.17. Source: UniProtKB

exit from mitosis

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of actin filament length

Inferred from mutant phenotype Ref.16. Source: UniProtKB

regulation of cell shape

Inferred from mutant phenotype Ref.11Ref.18. Source: UniProtKB

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from direct assay PubMed 17018287. Source: MGI

cell cortex

Inferred from direct assay Ref.6Ref.18. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from electronic annotation. Source: Ensembl

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from direct assay PubMed 17018287. Source: MGI

ruffle membrane

Inferred from direct assay Ref.6. Source: UniProtKB

stereocilium

Inferred from direct assay Ref.16. Source: UniProtKB

synapse

Inferred from direct assay PubMed 17018287. Source: MGI

   Molecular_functionRac GTPase binding

Inferred from direct assay Ref.6. Source: UniProtKB

actin binding

Inferred from direct assay Ref.6Ref.8Ref.15. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 821821Epidermal growth factor receptor kinase substrate 8
PRO_0000086995

Regions

Domain69 – 12961PH; first part
Domain381 – 41434PH; second part
Domain532 – 59160SH3
Region648 – 821174Effector region
Region679 – 69719Amphipathic helix
Region717 – 73721Helix bundle 1
Region751 – 7566Helix bundle 2
Region761 – 7666Helix bundle 3
Region765 – 78420Helix bundle 4
Compositional bias210 – 2134Poly-Pro
Compositional bias322 – 3254Poly-Pro
Compositional bias421 – 44020Pro-rich
Compositional bias620 – 65031Pro-rich
Compositional bias658 – 6636Poly-Ser

Amino acid modifications

Modified residue3171Phosphothreonine By similarity
Modified residue4751Phosphoserine By similarity
Modified residue6241Phosphoserine; by MAPK Ref.14
Modified residue6281Phosphothreonine; by MAPK Ref.14
Modified residue6581Phosphoserine Ref.13

Experimental info

Mutagenesis6241S → A: Does not detach from actin following BDNF treatment; when associated with A-628. Ref.14
Mutagenesis6241S → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-628. Ref.14
Mutagenesis6281T → A: Does not detach from actin following BDNF treatment; when associated with A-624. Ref.14
Mutagenesis6281T → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-624. Ref.14
Mutagenesis6891V → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. Ref.15
Mutagenesis6931L → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. Ref.15
Mutagenesis7061R → A: Impairs both actin capping and bundling activities. Ref.15
Mutagenesis7081F → A: Impairs both actin capping and bundling activities. Ref.15
Sequence conflict6521N → D in AAA16358. Ref.1
Sequence conflict6521N → D in AAH16890. Ref.3

Secondary structure

............. 821
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q08509 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 50F691FAC3EF1304

FASTA82191,737
        10         20         30         40         50         60 
MNGHMSNRSS GYGVYPSQLN GYGSSPPYSQ MDREHSSRTS AKALYEQRKN YARDSVSSVS 

        70         80         90        100        110        120 
DVSQYRVEHL TTFVLDRKDA MITVEDGIRK LKLLDAKGKV WTQDMILQVD DRAVSLIDLE 

       130        140        150        160        170        180 
SKNELENFPL NTISHCQAVV HACSYDSILA LVCKEPTQSK PDLHLFQCDE VKANLISEDI 

       190        200        210        220        230        240 
ESAISDSKGG KQKRRPEALR MIAKADPGIP PPPRAPAPVP PGTVTQVDVR SRVAAWSAWA 

       250        260        270        280        290        300 
ADQGDFEKPR QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR 

       310        320        330        340        350        360 
KKSKKSKRKG PGEGVLTLRA KPPPPDEFVD CFQKFKHGFN LLAKLKSHIQ NPSASDLVHF 

       370        380        390        400        410        420 
LFTPLNMVVQ ATGGPELASS VLSPLLTKDT VDFLNYTATA EERKLWMSLG DSWVKVRAEW 

       430        440        450        460        470        480 
PKEQFIPPYV PRFRNGWEPP MLNFMGAPTE QDMYQLAESV ANAEHQRKQD SKRLSTEHSN 

       490        500        510        520        530        540 
VSDYPPADGY AYSSSMYHRG PHADHGEAAM PFKSTPNHQV DRNYDAVKTQ PKKYAKSKYD 

       550        560        570        580        590        600 
FVARNSSELS VMKDDVLEIL DDRRQWWKVR NASGDSGFVP NNILDIMRTP ESGVGRADPP 

       610        620        630        640        650        660 
YTHTIQKQRT EYGLRSADTP SAPSPPPTPA PVPVPLPPSV PAPVSVPKVP ANVTRQNSSS 

       670        680        690        700        710        720 
SDSGGSIVRD SQRYKQLPVD RRKSQMEEVQ DELFQRLTIG RSAAQRKFHV PRQNVPVINI 

       730        740        750        760        770        780 
TYDSSPEEVK TWLQSKGFNP VTVNSLGVLN GAQLFSLNKD ELRSVCPEGA RVFNQITVQK 

       790        800        810        820 
AALEDSNGSS ELQEIMRRRQ EKISAAASDS GVESFDEGSS H 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"EPS8 and E3B1 transduce signals from Ras to Rac."
Scita G., Nordstrom J., Carbone R., Tenca P., Giardina G., Gutkind S., Bjarnegard M., Betsholtz C., Di Fiore P.P.
Nature 401:290-293(1999) [PubMed] [Europe PMC] [Abstract]
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]"Eps8 in the midst of GTPases."
Di Fiore P.P., Scita G.
Int. J. Biochem. Cell Biol. 34:1178-1183(2002) [PubMed] [Europe PMC] [Abstract]
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]"Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping."
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.
PLoS Biol. 8:E1000387-E1000387(2010) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L21671 mRNA. Translation: AAA16358.1.
AK149683 mRNA. Translation: BAE29023.1.
AK166156 mRNA. Translation: BAE38601.1.
BC016890 mRNA. Translation: AAH16890.1.
PIRS39983.
RefSeqNP_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.
UniGeneMm.235346.
Mm.412332.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AOJX-ray2.50A/B532-591[»]
1I07X-ray1.80A/B532-591[»]
1I0CX-ray2.00A/B532-591[»]
ProteinModelPortalQ08509.
SMRQ08509. Positions 59-188, 532-590, 698-783.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199491. 5 interactions.
DIPDIP-32858N.
IntActQ08509. 7 interactions.
MINTMINT-1506131.

PTM databases

PhosphoSiteQ08509.

Proteomic databases

PaxDbQ08509.
PRIDEQ08509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766.
ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766.
ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766.
GeneID13860.
KEGGmmu:13860.
UCSCuc009emz.1. mouse.

Organism-specific databases

CTD2059.
MGIMGI:104684. Eps8.

Phylogenomic databases

eggNOGNOG263108.
GeneTreeENSGT00390000003646.
HOGENOMHOG000060324.
HOVERGENHBG003090.
InParanoidQ3TM41.
KOK17277.
OMAWPKEQFI.
OrthoDBEOG7TMZR9.
TreeFamTF313069.

Gene expression databases

ArrayExpressQ08509.
BgeeQ08509.
GenevestigatorQ08509.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamPF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SSF50044. 1 hit.
PROSITEPS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEPS8. mouse.
EvolutionaryTraceQ08509.
NextBio284742.
PROQ08509.
SOURCESearch...

Entry information

Entry nameEPS8_MOUSE
AccessionPrimary (citable) accession number: Q08509
Secondary accession number(s): Q3TM41
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 130 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot