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Q12929

- EPS8_HUMAN

UniProt

Q12929 - EPS8_HUMAN

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Protein
Epidermal growth factor receptor kinase substrate 8
Gene
EPS8
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. Rac GTPase binding Source: UniProtKB
  2. SH3/SH2 adaptor activity Source: ProtInc
  3. actin binding Source: UniProtKB
  4. protein binding Source: IntAct

GO - Biological processi

  1. Rac protein signal transduction Source: UniProtKB
  2. actin crosslink formation Source: UniProtKB
  3. actin cytoskeleton reorganization Source: Ensembl
  4. actin filament bundle assembly Source: UniProtKB
  5. actin polymerization-dependent cell motility Source: UniProtKB
  6. adult locomotory behavior Source: Ensembl
  7. barbed-end actin filament capping Source: UniProtKB
  8. behavioral response to ethanol Source: Ensembl
  9. cell proliferation Source: ProtInc
  10. dendritic cell migration Source: UniProtKB
  11. epidermal growth factor receptor signaling pathway Source: ProtInc
  12. exit from mitosis Source: UniProtKB
  13. positive regulation of signal transduction Source: GOC
  14. regulation of actin filament length Source: UniProtKB
  15. regulation of cell shape Source: UniProtKB
  16. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

SignaLinkiQ12929.

Names & Taxonomyi

Protein namesi
Recommended name:
Epidermal growth factor receptor kinase substrate 8
Gene namesi
Name:EPS8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:3420. EPS8.

Subcellular locationi

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.

GO - Cellular componenti

  1. N-methyl-D-aspartate selective glutamate receptor complex Source: Ensembl
  2. cell cortex Source: UniProtKB
  3. cell junction Source: UniProtKB-KW
  4. extracellular vesicular exosome Source: UniProtKB
  5. growth cone Source: UniProtKB-SubCell
  6. postsynaptic density Source: Ensembl
  7. ruffle membrane Source: UniProtKB
  8. stereocilium Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Involvement in diseasei

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.

Organism-specific databases

PharmGKBiPA27839.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 822822Epidermal growth factor receptor kinase substrate 8
PRO_0000086994Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei317 – 3171Phosphothreonine By similarity
Modified residuei476 – 4761Phosphoserine1 Publication
Modified residuei625 – 6251Phosphoserine; by MAPK By similarity
Modified residuei629 – 6291Phosphothreonine; by MAPK By similarity
Modified residuei659 – 6591Phosphoserine By similarity

Post-translational modificationi

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.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ12929.
PaxDbiQ12929.
PRIDEiQ12929.

PTM databases

PhosphoSiteiQ12929.

Expressioni

Tissue specificityi

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.

Gene expression databases

ArrayExpressiQ12929.
BgeeiQ12929.
CleanExiHS_EPS8.
GenevestigatoriQ12929.

Organism-specific databases

HPAiHPA003897.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ALDH7A1P494192EBI-375576,EBI-726842
BAIAP2Q9UQB84EBI-375576,EBI-525456
CASKO149363EBI-375576,EBI-1215506

Protein-protein interaction databases

BioGridi108373. 47 interactions.
DIPiDIP-32859N.
IntActiQ12929. 41 interactions.
MINTiMINT-5004506.
STRINGi9606.ENSP00000281172.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi729 – 7379
Helixi741 – 7466
Beta strandi748 – 7503
Helixi752 – 7576
Helixi760 – 7667
Helixi770 – 78415

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2E8MNMR-A699-784[»]
ProteinModelPortaliQ12929.
SMRiQ12929. Positions 59-188, 533-589, 699-788.

Miscellaneous databases

EvolutionaryTraceiQ12929.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini69 – 12961PH; first part
Add
BLAST
Domaini381 – 41434PH; second part
Add
BLAST
Domaini531 – 59060SH3
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni649 – 822174Effector region By similarity
Add
BLAST
Regioni680 – 69819Amphipathic helix By similarity
Add
BLAST
Regioni718 – 73821Helix bundle 1 By similarity
Add
BLAST
Regioni752 – 7576Helix bundle 2 By similarity
Regioni762 – 7676Helix bundle 3 By similarity
Regioni766 – 78520Helix bundle 4 By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi421 – 44020Pro-rich
Add
BLAST
Compositional biasi615 – 65137Pro-rich
Add
BLAST
Compositional biasi659 – 6646Poly-Ser

Domaini

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.

Sequence similaritiesi

Belongs to the EPS8 family.
Contains 1 PH domain.
Contains 1 SH3 domain.

Keywords - Domaini

SH3 domain

Phylogenomic databases

eggNOGiNOG263108.
HOGENOMiHOG000060324.
HOVERGENiHBG003090.
InParanoidiQ12929.
KOiK17277.
OMAiIPPYVPR.
OrthoDBiEOG7TMZR9.
PhylomeDBiQ12929.
TreeFamiTF313069.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view]
PfamiPF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view]
SMARTiSM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view]
SUPFAMiSSF50044. SSF50044. 1 hit.
PROSITEiPS50002. SH3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q12929-1 [UniParc]FASTAAdd to Basket

« Hide

MNGHISNHPS SFGMYPSQMN GYGSSPTFSQ TDREHGSKTS AKALYEQRKN    50
YARDSVSSVS DISQYRVEHL TTFVLDRKDA MITVDDGIRK LKLLDAKGKV 100
WTQDMILQVD DRAVSLIDLE SKNELENFPL NTIQHCQAVM HSCSYDSVLA 150
LVCKEPTQNK PDLHLFQCDE VKANLISEDI ESAISDSKGG KQKRRPDALR 200
MISNADPSIP PPPRAPAPAP PGTVTQVDVR SRVAAWSAWA ADQGDFEKPR 250
QYHEQEETPE MMAARIDRDV QILNHILDDI EFFITKLQKA AEAFSELSKR 300
KKNKKGKRKG PGEGVLTLRA KPPPPDEFLD CFQKFKHGFN LLAKLKSHIQ 350
NPSAADLVHF LFTPLNMVVQ ATGGPELASS VLSPLLNKDT IDFLNYTVNG 400
DERQLWMSLG GTWMKARAEW PKEQFIPPYV PRFRNGWEPP MLNFMGATME 450
QDLYQLAESV ANVAEHQRKQ EIKRLSTEHS SVSEYHPADG YAFSSNIYTR 500
GSHLDQGEAA VAFKPTSNRH IDRNYEPLKT QPKKYAKSKY DFVARNNSEL 550
SVLKDDILEI LDDRKQWWKV RNASGDSGFV PNNILDIVRP PESGLGRADP 600
PYTHTIQKQR MEYGPRPADT PPAPSPPPTP APVPVPLPPS TPAPVPVSKV 650
PANITRQNSS SSDSGGSIVR DSQRHKQLPV DRRKSQMEEV QDELIHRLTI 700
GRSAAQKKFH VPRQNVPVIN ITYDSTPEDV KTWLQSKGFN PVTVNSLGVL 750
NGAQLFSLNK DELRTVCPEG ARVYSQITVQ KAALEDSSGS SELQEIMRRR 800
QEKISAAASD SGVESFDEGS SH 822
Length:822
Mass (Da):91,882
Last modified:November 1, 1996 - v1
Checksum:iAC5EB1D28B784B3B
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti761 – 7611D → E.
Corresponds to variant rs7137185 [ dbSNP | Ensembl ].
VAR_050971
Natural varianti806 – 8061A → S.
Corresponds to variant rs1802658 [ dbSNP | Ensembl ].
VAR_050972

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti73 – 731F → S in BAF84466. 1 Publication
Sequence conflicti128 – 1281F → S in BAF84466. 1 Publication
Sequence conflicti194 – 1941R → G in BAF84466. 1 Publication
Sequence conflicti205 – 2051A → S in BAF85620. 1 Publication
Sequence conflicti497 – 4971I → V in BAF85620. 1 Publication
Sequence conflicti631 – 6311A → V in AAH30010. 1 Publication
Sequence conflicti705 – 7051A → T in BAF85620. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS31753.1.
PIRiI38728.
RefSeqiNP_004438.3. NM_004447.5.
XP_005253397.1. XM_005253340.1.
XP_006719120.1. XM_006719057.1.
UniGeneiHs.591160.

Genome annotation databases

EnsembliENST00000281172; ENSP00000281172; ENSG00000151491.
ENST00000543523; ENSP00000441867; ENSG00000151491.
ENST00000543612; ENSP00000442388; ENSG00000151491.
GeneIDi2059.
KEGGihsa:2059.
UCSCiuc001rdb.3. human.

Polymorphism databases

DMDMi2833239.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS31753.1.
PIRi I38728.
RefSeqi NP_004438.3. NM_004447.5.
XP_005253397.1. XM_005253340.1.
XP_006719120.1. XM_006719057.1.
UniGenei Hs.591160.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2E8M NMR - A 699-784 [» ]
ProteinModelPortali Q12929.
SMRi Q12929. Positions 59-188, 533-589, 699-788.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108373. 47 interactions.
DIPi DIP-32859N.
IntActi Q12929. 41 interactions.
MINTi MINT-5004506.
STRINGi 9606.ENSP00000281172.

PTM databases

PhosphoSitei Q12929.

Polymorphism databases

DMDMi 2833239.

Proteomic databases

MaxQBi Q12929.
PaxDbi Q12929.
PRIDEi Q12929.

Protocols and materials databases

DNASUi 2059.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000281172 ; ENSP00000281172 ; ENSG00000151491 .
ENST00000543523 ; ENSP00000441867 ; ENSG00000151491 .
ENST00000543612 ; ENSP00000442388 ; ENSG00000151491 .
GeneIDi 2059.
KEGGi hsa:2059.
UCSCi uc001rdb.3. human.

Organism-specific databases

CTDi 2059.
GeneCardsi GC12M015673.
HGNCi HGNC:3420. EPS8.
HPAi HPA003897.
MIMi 600206. gene.
neXtProti NX_Q12929.
PharmGKBi PA27839.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG263108.
HOGENOMi HOG000060324.
HOVERGENi HBG003090.
InParanoidi Q12929.
KOi K17277.
OMAi IPPYVPR.
OrthoDBi EOG7TMZR9.
PhylomeDBi Q12929.
TreeFami TF313069.

Enzyme and pathway databases

SignaLinki Q12929.

Miscellaneous databases

ChiTaRSi EPS8. human.
EvolutionaryTracei Q12929.
GeneWikii EPS8.
GenomeRNAii 2059.
NextBioi 35464377.
PROi Q12929.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q12929.
Bgeei Q12929.
CleanExi HS_EPS8.
Genevestigatori Q12929.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
InterProi IPR011993. PH_like_dom.
IPR013625. PTB.
IPR006020. PTB/PI_dom.
IPR001452. SH3_domain.
[Graphical view ]
Pfami PF08416. PTB. 1 hit.
PF00018. SH3_1. 1 hit.
[Graphical view ]
SMARTi SM00462. PTB. 1 hit.
SM00326. SH3. 1 hit.
[Graphical view ]
SUPFAMi SSF50044. SSF50044. 1 hit.
PROSITEi PS50002. SH3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. 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.

Entry informationi

Entry nameiEPS8_HUMAN
AccessioniPrimary (citable) accession number: Q12929
Secondary accession number(s): A6NMC3
, A8K6W2, A8KA66, Q8N6J0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 129 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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