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Q12929

- EPS8_HUMAN

UniProt

Q12929 - EPS8_HUMAN

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
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    • History
      Entry version 130 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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. actin binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. Rac GTPase binding Source: UniProtKB
    4. SH3/SH2 adaptor activity Source: ProtInc

    GO - Biological processi

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

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

    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 8PRO_0000086994Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei317 – 3171PhosphothreonineBy similarity
    Modified residuei476 – 4761Phosphoserine1 Publication
    Modified residuei625 – 6251Phosphoserine; by MAPKBy similarity
    Modified residuei629 – 6291Phosphothreonine; by MAPKBy similarity
    Modified residuei659 – 6591PhosphoserineBy 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.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.By similarity1 Publication

    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.By similarity2 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

    1
    822
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12929.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini69 – 12961PH; first partAdd
    BLAST
    Domaini381 – 41434PH; second partAdd
    BLAST
    Domaini531 – 59060SH3PROSITE-ProRule annotationAdd
    BLAST

    Region

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

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi421 – 44020Pro-richAdd
    BLAST
    Compositional biasi615 – 65137Pro-richAdd
    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.By similarity
    The SH3 domain mediates interaction with SHB.

    Sequence similaritiesi

    Belongs to the EPS8 family.Curated
    Contains 1 PH domain.Curated
    Contains 1 SH3 domain.PROSITE-ProRule annotation

    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12929-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « 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
    Isoform 2 (identifier: Q12929-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-260: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:562
    Mass (Da):62,871
    Checksum:i8670D1025054D476
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti73 – 731F → S in BAF84466. (PubMed:14702039)Curated
    Sequence conflicti128 – 1281F → S in BAF84466. (PubMed:14702039)Curated
    Sequence conflicti194 – 1941R → G in BAF84466. (PubMed:14702039)Curated
    Sequence conflicti205 – 2051A → S in BAF85620. (PubMed:14702039)Curated
    Sequence conflicti497 – 4971I → V in BAF85620. (PubMed:14702039)Curated
    Sequence conflicti631 – 6311A → V in AAH30010. (PubMed:15489334)Curated
    Sequence conflicti705 – 7051A → T in BAF85620. (PubMed:14702039)Curated

    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

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 260260Missing in isoform 2. 1 PublicationVSP_056460Add
    BLAST

    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.
    AK301834 mRNA. Translation: BAG63278.1.
    AK316134 mRNA. Translation: BAH14505.1.
    AK316239 mRNA. Translation: BAH14610.1.
    AC022073 Genomic DNA. No translation available.
    AC073651 Genomic DNA. No translation available.
    AC092753 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96354.1.
    CH471094 Genomic DNA. Translation: EAW96355.1.
    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.
    ENST00000540613; ENSP00000441888; ENSG00000151491.
    ENST00000543523; ENSP00000441867; ENSG00000151491.
    ENST00000543612; ENSP00000442388; ENSG00000151491.
    GeneIDi2059.
    KEGGihsa:2059.
    UCSCiuc001rdb.3. human.

    Polymorphism databases

    DMDMi2833239.

    Keywords - Coding sequence diversityi

    Alternative splicing, 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 .
    AK301834 mRNA. Translation: BAG63278.1 .
    AK316134 mRNA. Translation: BAH14505.1 .
    AK316239 mRNA. Translation: BAH14610.1 .
    AC022073 Genomic DNA. No translation available.
    AC073651 Genomic DNA. No translation available.
    AC092753 Genomic DNA. No translation available.
    CH471094 Genomic DNA. Translation: EAW96354.1 .
    CH471094 Genomic DNA. Translation: EAW96355.1 .
    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 .
    ENST00000540613 ; ENSP00000441888 ; 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

    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] (ISOFORM 1).
    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] (ISOFORMS 1 AND 2).
      Tissue: Placenta, Testis, Tongue 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] (ISOFORM 1).
      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, B4DX66, Q8N6J0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 130 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