Q08509 (EPS8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Epidermal growth factor receptor kinase substrate 8

Gene names

Name:

Eps8

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	821 AA.
Sequence status	Complete.
Protein existence	Evidence 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.9 Ref.11 Ref.12 Ref.13 Ref.14
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.9 Ref.10 Ref.13 Ref.16
Subcellular location	Cytoplasm › cell cortex. Cell projection › ruffle membrane. Cell projection › growth cone By similarity. Cell projection › stereocilium. Note: Localizes to the midzone of dividing cells. Ref.6 Ref.13 Ref.15
Tissue specificity	Expressed in neuronal cell body and neurites, and prominently enriched in the axonal growth cone. Ref.11
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.12). 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.12). 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.15 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.11
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.13 Ref.14
Sequence similarities	Belongs to the EPS8 family. Contains 1 PH domain. Contains 1 SH3 domain.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Membrane
Domain	SH3 domain
Ligand	Actin-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rac protein signal transduction Inferred from direct assay Ref.6. Source: UniProtKB actin crosslink formation Inferred from direct assay Ref.12. Source: UniProtKB actin cytoskeleton reorganization Inferred from mutant phenotype PubMed 17018287. Source: MGI actin filament bundle assembly Inferred from direct assay Ref.12. 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.12. Source: UniProtKB behavioral response to ethanol Inferred from mutant phenotype PubMed 17018287. Source: MGI dendritic cell migration Inferred from mutant phenotype Ref.14. Source: UniProtKB exit from mitosis Inferred from mutant phenotype Ref.15. Source: UniProtKB regulation of cell shape Inferred from mutant phenotype Ref.9Ref.15. Source: UniProtKB regulation of mitotic prometaphase Inferred from mutant phenotype Ref.15. Source: UniProtKB
Cellular_component	N-methyl-D-aspartate selective glutamate receptor complex Inferred from direct assay PubMed 17018287. Source: MGI cell cortex Inferred from direct assay Ref.6Ref.15. Source: UniProtKB 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.13. Source: UniProtKB
Molecular_function	Rac GTPase binding Inferred from direct assay Ref.6. Source: UniProtKB actin binding Inferred from direct assay Ref.6Ref.8Ref.12. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ABI1	Q8IZP0	2	EBI-375596,EBI-375446	From a different organism.
Abi1	Q8CBW3	2	EBI-375596,EBI-375511
BAIAP2	Q9UQB8	8	EBI-375596,EBI-525456	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 821

821

Epidermal growth factor receptor kinase substrate 8

PRO_0000086995

Regions

Domain

69 – 129

61

PH; first part

Domain

381 – 414

34

PH; second part

Domain

532 – 591

60

SH3

Region

648 – 821

174

Effector region

Region

679 – 697

19

Amphipathic helix

Region

717 – 737

21

Helix bundle 1

Region

751 – 756

6

Helix bundle 2

Region

761 – 766

6

Helix bundle 3

Region

765 – 784

20

Helix bundle 4

Compositional bias

210 – 213

4

Poly-Pro

Compositional bias

322 – 325

4

Poly-Pro

Compositional bias

421 – 440

20

Pro-rich

Compositional bias

620 – 650

31

Pro-rich

Compositional bias

658 – 663

6

Poly-Ser

Amino acid modifications

Modified residue

475

1

Phosphoserine By similarity

Modified residue

624

1

Phosphoserine; by MAPK Ref.11

Modified residue

628

1

Phosphothreonine; by MAPK Ref.11

Experimental info

Mutagenesis

624

1

S → A: Does not detach from actin following BDNF treatment; when associated with A-628. Ref.11

Mutagenesis

624

1

S → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-628. Ref.11

Mutagenesis

628

1

T → A: Does not detach from actin following BDNF treatment; when associated with A-624. Ref.11

Mutagenesis

628

1

T → E: Mimicks phosphorylation state; promotes detachment from actin in absence of BDNF treatment; when associated with E-624. Ref.11

Mutagenesis

689

1

V → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. Ref.12

Mutagenesis

693

1

L → D: Abolishes barbed-end actin-binding without affecting actin bundling activity. Ref.12

Mutagenesis

706

1

R → A: Impairs both actin capping and bundling activities. Ref.12

Mutagenesis

708

1

F → A: Impairs both actin capping and bundling activities. Ref.12

Sequence conflict

652

1

N → D in AAA16358. Ref.1

Sequence conflict

652

1

N → D in AAH16890. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

821

Helix Strand Turn

Details...

Beta strand

534 – 539

6

Beta strand

556 – 559

4

Helix

561 – 563

3

Beta strand

566 – 570

5

Beta strand

576 – 580

5

Helix

581 – 583

3

Beta strand

584 – 587

4

Sequences

	Sequence		Length	Mass (Da)
	Q08509 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 50F691FAC3EF1304	FASTA	821	91,737
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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.

IPI

IPI00622390.

PIR

S39983.

RefSeq

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.

UniGene

Mm.235346.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q08509.

SMR

Q08509. Positions 59-188, 532-590, 698-783.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-32858N.

IntAct

Q08509. 3 interactions.

PTM databases

PhosphoSite

Q08509.

Proteomic databases

PaxDb

Q08509.

PRIDE

Q08509.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000058210; ENSMUSP00000052776; ENSMUSG00000015766.
ENSMUST00000100841; ENSMUSP00000098402; ENSMUSG00000015766.
ENSMUST00000111878; ENSMUSP00000107509; ENSMUSG00000015766.

GeneID

13860.

KEGG

mmu:13860.

Organism-specific databases

CTD

2059.

MGI

MGI:104684. Eps8.

Phylogenomic databases

eggNOG

NOG263108.

GeneTree

ENSGT00390000003646.

HOGENOM

HOG000060324.

HOVERGEN

HBG003090.

InParanoid

Q3TM41.

OMA

PEDVKTW.

OrthoDB

EOG42V8FP.

Gene expression databases

ArrayExpress

Q08509.

Bgee

Q08509.

Genevestigator

Q08509.

GermOnline

ENSMUSG00000015766. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTyr_interaction_dom.
IPR001452. SH3_domain.
[Graphical view]

Pfam

PF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]

SMART

SM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]

SUPFAM

SSF50044. SH3. 1 hit.

PROSITE

PS50003. PH_DOMAIN. False negative.
PS50002. SH3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

EPS8. mouse.

EvolutionaryTrace

Q08509.

NextBio

284742.

SOURCE

Search...

Entry information

Entry name

EPS8_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program