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Q08509 (EPS8_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 108. 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)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

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

General annotation (Comments)

Function

Upon binding to EGF receptor/EGFR enhances EGF-dependent mitogenic signals. Can bind multiple cellular targets. Ref.1

Subunit structure

Homodimer. Interacts with BAIAP2 By similarity. Interacts with SHB and LANCL1. Interacts with EGFR; mediates EPS8 phosphorylation. Ref.1 Ref.4 Ref.5 Ref.6

Domain

The SH3 domain mediates interaction with SHB By similarity.

Post-translational modification

Phosphorylated by several receptor tyrosine kinases. Ref.1

Sequence similarities

Belongs to the EPS8 family.

Contains 1 PH domain.

Contains 1 SH3 domain.

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.

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
Compositional bias210 – 2134Poly-Pro
Compositional bias322 – 3254Poly-Pro
Compositional bias421 – 44020Pro-rich
Compositional bias620 – 65031Pro-rich
Compositional bias658 – 6636Poly-Ser

Amino acid modifications

Modified residue4841Phosphotyrosine By similarity
Modified residue5241Phosphotyrosine By similarity
Modified residue6581Phosphoserine By similarity
Modified residue6601Phosphoserine By similarity
Modified residue6611Phosphoserine By similarity
Modified residue8101Phosphoserine By similarity
Modified residue8141Phosphoserine By similarity

Experimental info

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: 8404850] [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: 16141072] [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: 15489334] [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: 7537362] [Abstract]
Cited for: INTERACTION WITH SHB.
[5]"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: 19528316] [Abstract]
Cited for: INTERACTION WITH LANCL1.
[6]"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: 9303002] [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.
IPIIPI00622390.
PIRS39983.
RefSeqNP_031971.2. NM_007945.2.
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...

Protein-protein interaction databases

DIPDIP-32858N.
IntActQ08509. 3 interactions.
STRINGQ08509.

PTM databases

PhosphoSiteQ08509.

Proteomic databases

PRIDEQ08509.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTD2059.
MGIMGI:104684. Eps8.

Phylogenomic databases

eggNOGroNOG10217.
HOVERGENHBG003090.
InParanoidQ08509.
OrthoDBEOG42V8FP.

Gene expression databases

ArrayExpressQ08509.
BgeeQ08509.
GenevestigatorQ08509.
GermOnlineENSMUSG00000015766. Mus musculus.

Family and domain databases

InterProIPR011993. PH_type.
IPR013625. PTB.
IPR006020. PTyr_interaction_dom.
IPR001452. SH3_domain.
[Graphical view]
Gene3DG3DSA:2.30.29.30. PH_type. 1 hit.
PfamPF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMSSF50044. SH3. 1 hit.
PROSITEPS50003. PH_DOMAIN. False negative.
PS50002. SH3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

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: December 14, 2011
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families