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Q12929 (EPS8_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 126. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Epidermal growth factor receptor kinase substrate 8
Gene names
Name:EPS8
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length822 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.9 Ref.11

Subunit structure

Homodimer. Part of a complex consisting of ABI1, EPS8 and SOS1. Interacts with MYO15A and DFNB31. Interacts with LANCL1 By similarity. Interacts with EGFR; mediates EPS8 phosphorylation By similarity. Interacts with BAIAP2. Interacts with SHB. Ref.6 Ref.8

Subcellular location

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

Tissue specificity

Expressed in all tissues analyzed, including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Expressed in all epithelial and fibroblastic lines examined and in some, but not all, hematopoietic cells.

Domain

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

The SH3 domain mediates interaction with SHB.

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 By similarity.

Phosphorylation at Ser-625 and Thr-629 by MAPK following BDNF treatment promotes removal from actin and filopodia formation By similarity. Phosphorylated by several receptor tyrosine kinases.

Involvement in disease

Defects in EPS8 are associated with some cancers, such as pancreatic, oral squamous cell carcinomas or pituitary cancers. Contributes to cell transformation in response to growth factor treatment and is overexpressed in a number of tumors, indicating that EPS8 levels must be tightly regulated.

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
   Coding sequence diversityPolymorphism
   DomainSH3 domain
   LigandActin-binding
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRac protein signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

actin crosslink formation

Inferred from sequence or structural similarity. Source: UniProtKB

actin cytoskeleton reorganization

Inferred from electronic annotation. Source: Ensembl

actin filament bundle assembly

Inferred from sequence or structural similarity. Source: UniProtKB

actin polymerization-dependent cell motility

Inferred from sequence or structural similarity. Source: UniProtKB

adult locomotory behavior

Inferred from electronic annotation. Source: Ensembl

barbed-end actin filament capping

Inferred from sequence or structural similarity. Source: UniProtKB

behavioral response to ethanol

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement Ref.1. Source: ProtInc

dendritic cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

exit from mitosis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of signal transduction

Traceable author statement Ref.1. Source: GOC

regulation of actin filament length

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell shape

Inferred from sequence or structural similarity. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentN-methyl-D-aspartate selective glutamate receptor complex

Inferred from electronic annotation. Source: Ensembl

cell cortex

Inferred from sequence or structural similarity. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular vesicular exosome

Inferred from direct assay PubMed 11487543. Source: UniProtKB

growth cone

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic density

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from sequence or structural similarity. Source: UniProtKB

stereocilium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionRac GTPase binding

Inferred from sequence or structural similarity. Source: UniProtKB

SH3/SH2 adaptor activity

Traceable author statement Ref.1. Source: ProtInc

actin binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 822822Epidermal growth factor receptor kinase substrate 8
PRO_0000086994

Regions

Domain69 – 12961PH; first part
Domain381 – 41434PH; second part
Domain531 – 59060SH3
Region649 – 822174Effector region By similarity
Region680 – 69819Amphipathic helix By similarity
Region718 – 73821Helix bundle 1 By similarity
Region752 – 7576Helix bundle 2 By similarity
Region762 – 7676Helix bundle 3 By similarity
Region766 – 78520Helix bundle 4 By similarity
Compositional bias421 – 44020Pro-rich
Compositional bias615 – 65137Pro-rich
Compositional bias659 – 6646Poly-Ser

Amino acid modifications

Modified residue3171Phosphothreonine By similarity
Modified residue4761Phosphoserine Ref.14
Modified residue6251Phosphoserine; by MAPK By similarity
Modified residue6291Phosphothreonine; by MAPK By similarity
Modified residue6591Phosphoserine By similarity

Natural variations

Natural variant7611D → E.
Corresponds to variant rs7137185 [ dbSNP | Ensembl ].
VAR_050971
Natural variant8061A → S.
Corresponds to variant rs1802658 [ dbSNP | Ensembl ].
VAR_050972

Experimental info

Sequence conflict731F → S in BAF84466. Ref.2
Sequence conflict1281F → S in BAF84466. Ref.2
Sequence conflict1941R → G in BAF84466. Ref.2
Sequence conflict2051A → S in BAF85620. Ref.2
Sequence conflict4971I → V in BAF85620. Ref.2
Sequence conflict6311A → V in AAH30010. Ref.5
Sequence conflict7051A → T in BAF85620. Ref.2

Secondary structure

............. 822
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q12929 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: AC5EB1D28B784B3B

FASTA82291,882
        10         20         30         40         50         60 
MNGHISNHPS SFGMYPSQMN GYGSSPTFSQ TDREHGSKTS AKALYEQRKN YARDSVSSVS 

        70         80         90        100        110        120 
DISQYRVEHL TTFVLDRKDA MITVDDGIRK LKLLDAKGKV WTQDMILQVD DRAVSLIDLE 

       130        140        150        160        170        180 
SKNELENFPL NTIQHCQAVM HSCSYDSVLA LVCKEPTQNK PDLHLFQCDE VKANLISEDI 

       190        200        210        220        230        240 
ESAISDSKGG KQKRRPDALR MISNADPSIP PPPRAPAPAP PGTVTQVDVR SRVAAWSAWA 

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

       310        320        330        340        350        360 
KKNKKGKRKG PGEGVLTLRA KPPPPDEFLD CFQKFKHGFN LLAKLKSHIQ NPSAADLVHF 

       370        380        390        400        410        420 
LFTPLNMVVQ ATGGPELASS VLSPLLNKDT IDFLNYTVNG DERQLWMSLG GTWMKARAEW 

       430        440        450        460        470        480 
PKEQFIPPYV PRFRNGWEPP MLNFMGATME QDLYQLAESV ANVAEHQRKQ EIKRLSTEHS 

       490        500        510        520        530        540 
SVSEYHPADG YAFSSNIYTR GSHLDQGEAA VAFKPTSNRH IDRNYEPLKT QPKKYAKSKY 

       550        560        570        580        590        600 
DFVARNNSEL SVLKDDILEI LDDRKQWWKV RNASGDSGFV PNNILDIVRP PESGLGRADP 

       610        620        630        640        650        660 
PYTHTIQKQR MEYGPRPADT PPAPSPPPTP APVPVPLPPS TPAPVPVSKV PANITRQNSS 

       670        680        690        700        710        720 
SSDSGGSIVR DSQRHKQLPV DRRKSQMEEV QDELIHRLTI GRSAAQKKFH VPRQNVPVIN 

       730        740        750        760        770        780 
ITYDSTPEDV KTWLQSKGFN PVTVNSLGVL NGAQLFSLNK DELRTVCPEG ARVYSQITVQ 

       790        800        810        820 
KAALEDSSGS SELQEIMRRR QEKISAAASD SGVESFDEGS SH 

« Hide

References

« Hide 'large scale' references
[1]"Evolutionary conservation of the EPS8 gene and its mapping to human chromosome 12q23-q24."
Wong W.T., Carlomagno F., Druck T., Barletta C., Croce C.M., Huebner K., Kraus M.H., di Fiore P.P.
Oncogene 9:3057-3061(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Placenta and Trachea.
[3]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
Tissue: Brain.
[6]"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.
[7]"Overexpression of p97Eps8 leads to cellular transformation: implication of pleckstrin homology domain in p97Eps8-mediated ERK activation."
Maa M.C., Hsieh C.Y., Leu T.H.
Oncogene 20:106-112(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[8]"IRSp53/Eps8 complex is important for positive regulation of Rac and cancer cell motility/invasiveness."
Funato Y., Terabayashi T., Suenaga N., Seiki M., Takenawa T., Miki H.
Cancer Res. 64:5237-5244(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP2.
[9]"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.
[10]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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.
[12]"Eps8 is increased in pancreatic cancer and required for dynamic actin-based cell protrusions and intercellular cytoskeletal organization."
Welsch T., Endlich K., Giese T., Buchler M.W., Schmidt J.
Cancer Lett. 255:205-218(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[13]"Eps8 decreases chemosensitivity and affects survival of cervical cancer patients."
Chen Y.J., Shen M.R., Chen Y.J., Maa M.C., Leu T.H.
Mol. Cancer Ther. 7:1376-1385(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[14]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Role for EPS8 in squamous carcinogenesis."
Wang H., Patel V., Miyazaki H., Gutkind J.S., Yeudall W.A.
Carcinogenesis 30:165-174(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[16]"Epidermal growth factor receptor pathway substrate 8 is overexpressed in human pituitary tumors: role in proliferation and survival."
Xu M., Shorts-Cary L., Knox A.J., Kleinsmidt-DeMasters B., Lillehei K., Wierman M.E.
Endocrinology 150:2064-2071(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[17]"Upregulation of Eps8 in oral squamous cell carcinoma promotes cell migration and invasion through integrin-dependent Rac1 activation."
Yap L.F., Jenei V., Robinson C.M., Moutasim K., Benn T.M., Threadgold S.P., Lopes V., Wei W., Thomas G.J., Paterson I.C.
Oncogene 28:2524-2534(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN CANCER.
[18]"Solution structure of the C-terminal SAM-domain of epidermal growth receptor pathway substrate 8."
RIKEN structural genomics initiative (RSGI)
Submitted (JUL-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 699-788.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U12535 mRNA. Translation: AAA62280.1.
AK291777 mRNA. Translation: BAF84466.1.
AK292931 mRNA. Translation: BAF85620.1.
AC092753 Genomic DNA. No translation available.
CH471094 Genomic DNA. Translation: EAW96354.1.
BC030010 mRNA. Translation: AAH30010.1.
PIRI38728.
RefSeqNP_004438.3. NM_004447.5.
XP_005253397.1. XM_005253340.1.
UniGeneHs.591160.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2E8MNMR-A699-784[»]
ProteinModelPortalQ12929.
SMRQ12929. Positions 59-188, 533-589, 699-788.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108373. 47 interactions.
DIPDIP-32859N.
IntActQ12929. 41 interactions.
MINTMINT-5004506.
STRING9606.ENSP00000281172.

PTM databases

PhosphoSiteQ12929.

Polymorphism databases

DMDM2833239.

Proteomic databases

PaxDbQ12929.
PRIDEQ12929.

Protocols and materials databases

DNASU2059.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000281172; ENSP00000281172; ENSG00000151491.
ENST00000543523; ENSP00000441867; ENSG00000151491.
ENST00000543612; ENSP00000442388; ENSG00000151491.
GeneID2059.
KEGGhsa:2059.
UCSCuc001rdb.3. human.

Organism-specific databases

CTD2059.
GeneCardsGC12M015673.
HGNCHGNC:3420. EPS8.
HPAHPA003897.
MIM600206. gene.
neXtProtNX_Q12929.
PharmGKBPA27839.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263108.
HOGENOMHOG000060324.
HOVERGENHBG003090.
InParanoidQ12929.
KOK17277.
OMAWPKEQFI.
OrthoDBEOG7TMZR9.
PhylomeDBQ12929.
TreeFamTF313069.

Enzyme and pathway databases

SignaLinkQ12929.

Gene expression databases

ArrayExpressQ12929.
BgeeQ12929.
CleanExHS_EPS8.
GenevestigatorQ12929.

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. human.
EvolutionaryTraceQ12929.
GeneWikiEPS8.
GenomeRNAi2059.
NextBio35464377.
PROQ12929.
SOURCESearch...

Entry information

Entry nameEPS8_HUMAN
AccessionPrimary (citable) accession number: Q12929
Secondary accession number(s): A6NMC3 expand/collapse secondary AC list , A8K6W2, A8KA66, Q8N6J0
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

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PDB cross-references

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MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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