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Q03173

- ENAH_MOUSE

UniProt

Q03173 - ENAH_MOUSE

Protein

Protein enabled homolog

Gene

Enah

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (23 Apr 2003)
      Previous versions | rss
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    Functioni

    Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation.4 Publications

    GO - Molecular functioni

    1. profilin binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. SH3 domain binding Source: MGI

    GO - Biological processi

    1. actin cytoskeleton organization Source: MGI
    2. actin filament organization Source: UniProtKB
    3. actin polymerization or depolymerization Source: MGI
    4. axon guidance Source: MGI
    5. cellular component movement Source: UniProtKB
    6. intracellular transport Source: InterPro
    7. neural tube closure Source: MGI

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Neurogenesis

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_221567. Signaling by Robo receptor.
    REACT_225768. Generation of second messenger molecules.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein enabled homolog
    Alternative name(s):
    NPC-derived proline-rich protein 1
    Short name:
    NDPP-1
    Gene namesi
    Name:Enah
    Synonyms:Mena, Ndpp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:108360. Enah.

    Subcellular locationi

    Cytoplasm 3 Publications. Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell junctionsynapse By similarity. Cell junctionfocal adhesion By similarity
    Note: Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at filopodial tips with a number of other proteins including vinculin and zyxlin. Colocalizes with N-WASP at the leading edge. Colocalizes with GPHN and PFN at synapses By similarity.By similarity

    GO - Cellular componenti

    1. actin cytoskeleton Source: MGI
    2. cytosol Source: Reactome
    3. filopodium Source: MGI
    4. focal adhesion Source: UniProtKB
    5. lamellipodium Source: MGI
    6. stress fiber Source: MGI
    7. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

    Pathology & Biotechi

    Disruption phenotypei

    Mutant animals are viable and recovered in the appropriate Mendelian ratios. they are smaller than their littermates until adulthood and exhibit abnormal cage behavior, including reduced activity.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi255 – 2551S → A: No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. Loss of cell mobility function; when associated with A-637. 1 Publication
    Mutagenesisi255 – 2551S → D: No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function; when associated with D-637. 1 Publication
    Mutagenesisi637 – 6371S → A: No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with A-255. 1 Publication
    Mutagenesisi637 – 6371S → D: No change in subcellular location nor colocalization with vinculin at focal adhesions nor with N-WASP at the leading edge. No loss of cell mobility function. when associated with D-255. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 802802Protein enabled homologPRO_0000086972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei144 – 1441Phosphoserine1 Publication
    Modified residuei255 – 2551Phosphoserine; by PKA1 Publication
    Modified residuei557 – 5571Phosphotyrosine1 Publication
    Modified residuei738 – 7381PhosphoserineBy similarity
    Modified residuei740 – 7401PhosphoserineBy similarity

    Post-translational modificationi

    NTN1-induced PKA phosphorylation on Ser-255 directly parallels the formation of filopodial protrusions.3 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ03173.
    PaxDbiQ03173.
    PRIDEiQ03173.

    PTM databases

    PhosphoSiteiQ03173.

    Expressioni

    Tissue specificityi

    Expressed in heart and testis, lower levels in lung, skeletal muscle, kidney, pancreas and brain. Isoform 5 is expressed exclusively in the brain. Isoform 2 is expressed predominantly in brain, testis, ovary and fat. In the brain, isoforms 2 and 5 are expressed at highest levels in the hippocampus, cortex and midbrain, and at lowest levels in the striatum and cerebellum. Isoform 6 is expressed in brain and spleen.3 Publications

    Developmental stagei

    At 8.5 dpc, particularly enriched in the neuroepithelium, the forebrain and the somites. Highly expressed in the edges of the neural folds. By 10.5 dpc, detected in the brain, dorsal root ganglia (DRG), somites and limb buds. Highly expressed in the branchial and pharyngeal arches, neural crest-derived structures that give rise to portions of the face and neck. At 11 dpc, isoform 2, isoform 3 and isoform 5 are expressed in embryonic brain (at protein level). Expression of isoform 3 decreases steadily and becomes almost undetectable by 16 dpc, while expression of isoform 5 begins to increase from 13 dpc and peaks between 16 and 18 dpc (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ03173.
    BgeeiQ03173.
    CleanExiMM_ENAH.
    GenevestigatoriQ03173.

    Interactioni

    Subunit structurei

    Homotetramer By similarity. Interacts with APBB1IP, APBB1, PFN1 and ROBO4. Isoforms, containing the polyproline-rich regions with PPLP motifs, bind the WW domain of APBB1IP. Isoforms, containing the PPSY motif, bind, in vitro, to the WW2 and WW3 domains of NEDD4 and to the WW1 domain of YAP1. Binds the SH3 domain of BAIAP2-alpha but only after the autoinhibitory region of BAIAP2-alpha has been blocked by interaction with CDC42. Interacts, via the EVH1/WH1 domain, with the Pro-rich domains from VCL, ZYX and Listeria monocytogenes actA and with TES (via LIM domain). The TES LIM domain and the Pro-rich domains from VCL or ZYX compete for the same binding site. Interaction with ZYX is important for targeting ENAH to focal adhesions and enhances production of actin-rich structures at the apical surface of cells. Interacts, through the Pro-rich region, with the C-terminal SH3 domain of DNMPB. Binds GPHN. Heterotrimer with TES and ACTL7A By similarity. Interacts with FAT1 (via EVH1 domains).By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    BAIAP2Q9UQB83EBI-6083294,EBI-525456From a different organism.

    Protein-protein interaction databases

    BioGridi199446. 10 interactions.
    DIPiDIP-29359N.
    IntActiQ03173. 7 interactions.
    MINTiMINT-1215621.

    Structurei

    Secondary structure

    1
    802
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 1715
    Turni18 – 214
    Beta strandi22 – 254
    Helixi26 – 283
    Beta strandi33 – 408
    Turni41 – 444
    Beta strandi45 – 528
    Turni53 – 553
    Beta strandi58 – 647
    Beta strandi74 – 818
    Beta strandi86 – 938
    Helixi94 – 11118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EVHX-ray1.80A1-112[»]
    4CC3X-ray1.97B/D/F/H547-558[»]
    ProteinModelPortaliQ03173.
    SMRiQ03173. Positions 1-113.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ03173.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 111111WH1PROSITE-ProRule annotationAdd
    BLAST
    Repeati175 – 17951
    Repeati180 – 18452
    Repeati185 – 18953
    Repeati190 – 19454
    Repeati195 – 19955
    Repeati200 – 20456
    Repeati205 – 20957

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni175 – 209357 X 5 AA tandem repeats of [LM]-E-[QR]-[EQ]-[QR]Add
    BLAST
    Regioni623 – 799177EVH2Add
    BLAST
    Regioni623 – 64321EVH2 block AAdd
    BLAST
    Regioni674 – 69118EVH2 block BAdd
    BLAST
    Regioni765 – 79935EVH2 block CAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili154 – 258105Sequence AnalysisAdd
    BLAST
    Coiled coili767 – 79731Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi632 – 6354KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi269 – 605337Pro-richAdd
    BLAST

    Domaini

    The EVH2 domain is comprised of 3 regions. Block A is a thymosin-like domain required for G-actin binding. The KLKR motif within this block is essential for the G-actin binding and for actin polymerization. Block B is required for F-actin binding and subcellular location, and Block C for tetramerization.

    Sequence similaritiesi

    Belongs to the Ena/VASP family.Curated
    Contains 1 WH1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat, SH3-binding

    Phylogenomic databases

    eggNOGiNOG289321.
    GeneTreeiENSGT00730000110272.
    HOGENOMiHOG000013015.
    HOVERGENiHBG006655.
    InParanoidiQ03173.
    KOiK05746.
    PhylomeDBiQ03173.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view]
    PfamiPF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view]
    SMARTiSM00160. RanBD. 1 hit.
    SM00461. WH1. 1 hit.
    [Graphical view]
    PROSITEiPS50229. WH1. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 5 (identifier: Q03173-1) [UniParc]FASTAAdd to Basket

    Also known as: Neural variant Mena+++, 140 kDa isoform

    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

    MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG    50
    RKIQDHQVVI NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF 100
    ASAMMHALEV LNSQEAAQSK VTATQDSTNL RCIFCGPTLP RQNSQLPAQV 150
    QNGPSQEELE IQRRQLQEQQ RQKELERERM ERERLERERL ERERLERERL 200
    EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ LEREQVEWER 250
    ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD 300
    YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN 350
    SRPSSPVNTP SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP 400
    VLPVCVSSPV PQMPPSPTAP NGSLDSVTYP VSPPPTSGPA APPPPPPPPP 450
    PPPPPPLPPP PLPPLASLSH CGSQASPPPG TPLASTPSSK PSVLPSPSAG 500
    APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL GPPAPPPPPP 550
    LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP 600
    APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT 650
    GSVSLASSKA DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE 700
    QKEDRNEDAE PITAKAPSTS TPEPTRKPWE RTNTMNGSKS PVISRPKSTP 750
    SSQPSANGVQ TEGLDYDRLK QDILDEMRKE LAKLKEELID AIRQELSKSN 800
    TA 802
    Length:802
    Mass (Da):85,844
    Last modified:April 23, 2003 - v2
    Checksum:i592BB975EE20F77F
    GO
    Isoform 1 (identifier: Q03173-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-412: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:390
    Mass (Da):39,306
    Checksum:i1AA5DDB306450847
    GO
    Isoform 2 (identifier: Q03173-3) [UniParc]FASTAAdd to Basket

    Also known as: Mena, 80 kDa isoform

    The sequence of this isoform differs from the canonical sequence as follows:
         117-135: Missing.
         259-500: Missing.

    Show »
    Length:541
    Mass (Da):59,643
    Checksum:i19B25FD175DF0451
    GO
    Isoform 3 (identifier: Q03173-4) [UniParc]FASTAAdd to Basket

    Also known as: Neural variant Mena+

    The sequence of this isoform differs from the canonical sequence as follows:
         117-135: Missing.

    Note: Phosphorylated during neural development.

    Show »
    Length:783
    Mass (Da):83,776
    Checksum:i5E610BE7FDDA97FE
    GO
    Isoform 4 (identifier: Q03173-5) [UniParc]FASTAAdd to Basket

    Also known as: Neural variant Mena++

    The sequence of this isoform differs from the canonical sequence as follows:
         117-131: Missing.
         132-135: CIFC → VFYL

    Show »
    Length:787
    Mass (Da):84,299
    Checksum:i18C228F070EDCCF2
    GO
    Isoform 6 (identifier: Q03173-6) [UniParc]FASTAAdd to Basket

    Also known as: Mena(S)

    The sequence of this isoform differs from the canonical sequence as follows:
         117-135: Missing.
         259-500: Missing.
         561-594: Missing.

    Show »
    Length:507
    Mass (Da):56,357
    Checksum:iFA0C43AAD240503C
    GO

    Sequence cautioni

    The sequence BAA01570.1 differs from that shown. Reason: Frameshift at several positions.
    Isoform 1 : The sequence BAA01570.1 differs from that shown. Reason: Frameshift at several positions.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti500 – 5001G → A in BAA01570. (PubMed:1420303)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 412412Missing in isoform 1. 1 PublicationVSP_007255Add
    BLAST
    Alternative sequencei117 – 13519Missing in isoform 2, isoform 3 and isoform 6. 2 PublicationsVSP_007259Add
    BLAST
    Alternative sequencei117 – 13115Missing in isoform 4. 1 PublicationVSP_007257Add
    BLAST
    Alternative sequencei132 – 1354CIFC → VFYL in isoform 4. 1 PublicationVSP_007258
    Alternative sequencei259 – 500242Missing in isoform 2 and isoform 6. 2 PublicationsVSP_007260Add
    BLAST
    Alternative sequencei561 – 59434Missing in isoform 6. CuratedVSP_010565Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10727 mRNA. Translation: BAA01570.1. Frameshift.
    U72520 mRNA. Translation: AAC52863.1.
    U72521 mRNA. Translation: AAC52864.1.
    U72522 mRNA. Translation: AAC52865.1.
    U72523 mRNA. Translation: AAC52866.1.
    BC062927 mRNA. Translation: AAH62927.1.
    PIRiS27200.
    RefSeqiNP_001076590.1. NM_001083121.2. [Q03173-3]
    UniGeneiMm.389224.
    Mm.87759.

    Genome annotation databases

    EnsembliENSMUST00000111025; ENSMUSP00000106654; ENSMUSG00000022995. [Q03173-6]
    GeneIDi13800.
    KEGGimmu:13800.
    UCSCiuc007dxs.1. mouse. [Q03173-3]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D10727 mRNA. Translation: BAA01570.1 . Frameshift.
    U72520 mRNA. Translation: AAC52863.1 .
    U72521 mRNA. Translation: AAC52864.1 .
    U72522 mRNA. Translation: AAC52865.1 .
    U72523 mRNA. Translation: AAC52866.1 .
    BC062927 mRNA. Translation: AAH62927.1 .
    PIRi S27200.
    RefSeqi NP_001076590.1. NM_001083121.2. [Q03173-3 ]
    UniGenei Mm.389224.
    Mm.87759.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EVH X-ray 1.80 A 1-112 [» ]
    4CC3 X-ray 1.97 B/D/F/H 547-558 [» ]
    ProteinModelPortali Q03173.
    SMRi Q03173. Positions 1-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199446. 10 interactions.
    DIPi DIP-29359N.
    IntActi Q03173. 7 interactions.
    MINTi MINT-1215621.

    PTM databases

    PhosphoSitei Q03173.

    Proteomic databases

    MaxQBi Q03173.
    PaxDbi Q03173.
    PRIDEi Q03173.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000111025 ; ENSMUSP00000106654 ; ENSMUSG00000022995 . [Q03173-6 ]
    GeneIDi 13800.
    KEGGi mmu:13800.
    UCSCi uc007dxs.1. mouse. [Q03173-3 ]

    Organism-specific databases

    CTDi 55740.
    MGIi MGI:108360. Enah.

    Phylogenomic databases

    eggNOGi NOG289321.
    GeneTreei ENSGT00730000110272.
    HOGENOMi HOG000013015.
    HOVERGENi HBG006655.
    InParanoidi Q03173.
    KOi K05746.
    PhylomeDBi Q03173.

    Enzyme and pathway databases

    Reactomei REACT_221567. Signaling by Robo receptor.
    REACT_225768. Generation of second messenger molecules.

    Miscellaneous databases

    ChiTaRSi ENAH. mouse.
    EvolutionaryTracei Q03173.
    NextBioi 284558.
    PROi Q03173.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q03173.
    Bgeei Q03173.
    CleanExi MM_ENAH.
    Genevestigatori Q03173.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR011993. PH_like_dom.
    IPR000156. Ran_bind_dom.
    IPR014885. VASP_tetra.
    IPR000697. WH1/EVH1.
    [Graphical view ]
    Pfami PF08776. VASP_tetra. 1 hit.
    PF00568. WH1. 1 hit.
    [Graphical view ]
    SMARTi SM00160. RanBD. 1 hit.
    SM00461. WH1. 1 hit.
    [Graphical view ]
    PROSITEi PS50229. WH1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Identification of a developmentally regulated gene in the mouse central nervous system which encodes a novel proline rich protein."
      Sazuka T., Tomooka Y., Kathju S., Ikawa Y., Noda M., Kumar S.
      Biochim. Biophys. Acta 1132:240-248(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Brain.
    2. "Mena, a relative of VASP and Drosophila Enabled, is implicated in the control of microfilament dynamics."
      Gertler F.B., Niebuhr K., Reinhard M., Wehland J., Soriano P.
      Cell 87:227-239(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5), FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ROLE IN L.MONOCYTOGENES MOBILITY, MISCELLANEOUS, INTERACTION WITH PFN1.
      Tissue: Brain.
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Brain.
    4. "The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled."
      Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T., Sudol M.
      J. Biol. Chem. 272:32869-32877(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBB1; NEDD4 AND YAP1.
    5. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, DISRUPTION PHENOTYPE.
    6. "Critical roles of phosphorylation and actin binding motifs, but not the central proline-rich region, for Ena/vasodilator-stimulated phosphoprotein (VASP) function during cell migration."
      Loureiro J.J., Rubinson D.A., Bear J.E., Baltus G.A., Kwiatkowski A.V., Gertler F.B.
      Mol. Biol. Cell 13:2533-2546(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-255 AND SER-637.
    7. "Robo4 is a vascular-specific receptor that inhibits endothelial migration."
      Park K.W., Morrison C.M., Sorensen L.K., Jones C.A., Rao Y., Chien C.-B., Wu J.Y., Urness L.D., Li D.Y.
      Dev. Biol. 261:251-267(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ROBO4.
      Strain: FVB/N.
    8. "Abl interactor 1 promotes tyrosine 296 phosphorylation of mammalian enabled (Mena) by c-Abl kinase."
      Tani K., Sato S., Sukezane T., Kojima H., Hirose H., Hanafusa H., Shishido T.
      J. Biol. Chem. 278:21685-21692(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 6), PHOSPHORYLATION AT TYR-557, INTERACTION WITH ABI1.
    9. "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton."
      Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.
      J. Biol. Chem. 278:49031-49043(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DNMBP.
    10. "Mammalian Fat1 cadherin regulates actin dynamics and cell-cell contact."
      Tanoue T., Takeichi M.
      J. Cell Biol. 165:517-528(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FAT1.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    12. "Critical role of Ena/VASP proteins for filopodia formation in neurons and in function downstream of netrin-1."
      Lebrand C., Dent E.W., Strasser G.A., Lanier L.M., Krause M., Svitkina T.M., Borisy G.G., Gertler F.B.
      Neuron 42:37-49(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION AT SER-255.
    13. "PREL1 provides a link from Ras signalling to the actin cytoskeleton via Ena/VASP proteins."
      Jenzora A., Behrendt B., Small J.V., Wehland J., Stradal T.E.
      FEBS Lett. 579:455-463(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBB1IP.
    14. "Structure of the enabled/VASP homology 1 domain-peptide complex: a key component in the spatial control of actin assembly."
      Prehoda K.E., Lee D.J., Lim W.A.
      Cell 97:471-480(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-112 IN COMPLEX WITH PRO-RICH PEPTIDE OF L.MONOCYTOGENES ACTA.

    Entry informationi

    Entry nameiENAH_MOUSE
    AccessioniPrimary (citable) accession number: Q03173
    Secondary accession number(s): P70430
    , P70431, P70432, P70433, Q5D053
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: April 23, 2003
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3