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Q8N8S7

- ENAH_HUMAN

UniProt

Q8N8S7 - ENAH_HUMAN

Protein

Protein enabled homolog

Gene

ENAH

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      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 By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. WW domain binding Source: UniProtKB

    GO - Biological processi

    1. actin polymerization or depolymerization Source: Ensembl
    2. axon guidance Source: Reactome
    3. intracellular transport Source: InterPro
    4. neural tube closure Source: Ensembl
    5. T cell receptor signaling pathway Source: Reactome

    Keywords - Ligandi

    Actin-binding

    Enzyme and pathway databases

    ReactomeiREACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein enabled homolog
    Gene namesi
    Name:ENAH
    Synonyms:MENA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:18271. ENAH.

    Subcellular locationi

    Cytoplasm. Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Cell projectionfilopodium By similarity. Cell junctionsynapse By similarity. Cell junctionfocal adhesion
    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. cell junction Source: HPA
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. filopodium Source: UniProtKB-SubCell
    5. focal adhesion Source: HPA
    6. lamellipodium Source: UniProtKB-SubCell
    7. plasma membrane Source: HPA
    8. stress fiber Source: Ensembl
    9. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA38517.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 591591Protein enabled homologPRO_0000086971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei125 – 1251Phosphoserine3 Publications
    Modified residuei265 – 2651Phosphoserine; by PKABy similarity
    Modified residuei506 – 5061Phosphoserine2 Publications
    Modified residuei508 – 5081Phosphoserine2 Publications

    Post-translational modificationi

    NTN1-induced PKA phosphorylation on Ser-265 directly parallels the formation of filopodial protrusions.By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ8N8S7.
    PaxDbiQ8N8S7.
    PRIDEiQ8N8S7.

    PTM databases

    PhosphoSiteiQ8N8S7.

    Expressioni

    Tissue specificityi

    Expressed in myoepithelia of parotid, breast, bronchial glands and sweat glands. Expressed in colon-rectum muscolaris mucosae epithelium, pancreas acinar ductal epithelium, endometrium epithelium, prostate fibromuscolar stroma and placenta vascular media. Overexpressed in a majority of breast cancer cell lines and primary breast tumor lesions.1 Publication

    Gene expression databases

    BgeeiQ8N8S7.
    CleanExiHS_ENAH.
    GenevestigatoriQ8N8S7.

    Organism-specific databases

    HPAiHPA028448.
    HPA028696.

    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 domains). 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 By similarity. Interacts with FAT1 (via EVH1 domains) By similarity. Heterotrimer with TES and ACTL7A.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FAT1Q145172EBI-2834410,EBI-1171918

    Protein-protein interaction databases

    BioGridi120858. 21 interactions.
    IntActiQ8N8S7. 12 interactions.
    MINTiMINT-3041121.
    STRINGi9606.ENSP00000355809.

    Structurei

    Secondary structure

    1
    591
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 1714
    Turni18 – 214
    Beta strandi22 – 254
    Helixi26 – 283
    Beta strandi33 – 408
    Turni41 – 444
    Beta strandi45 – 528
    Turni53 – 553
    Beta strandi58 – 636
    Beta strandi74 – 818
    Beta strandi86 – 938
    Helixi94 – 11118

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2HO2X-ray1.33B347-356[»]
    2IYBX-ray2.35A/B/C/D1-113[»]
    2XQNX-ray2.62M1-116[»]
    ProteinModelPortaliQ8N8S7.
    SMRiQ8N8S7. Positions 1-113.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8N8S7.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 111111WH1PROSITE-ProRule annotationAdd
    BLAST
    Repeati156 – 16051
    Repeati161 – 16552
    Repeati166 – 17053
    Repeati171 – 17554
    Repeati176 – 18055
    Repeati181 – 18556
    Repeati186 – 19057
    Repeati191 – 19558
    Repeati196 – 20059

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni156 – 200459 X 5 AA tandem repeats of [LMQ]-E-[QR]-E-[QR]Add
    BLAST
    Regioni391 – 588198EVH2Add
    BLAST
    Regioni391 – 41121EVH2 block AAdd
    BLAST
    Regioni442 – 45918EVH2 block BAdd
    BLAST
    Regioni554 – 58835EVH2 block CAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili135 – 265131Sequence AnalysisAdd
    BLAST
    Coiled coili557 – 58731Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi400 – 4034KLKR

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi310 – 37364Pro-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.
    HOVERGENiHBG006655.
    KOiK05746.
    OrthoDBiEOG72JWGQ.
    PhylomeDBiQ8N8S7.
    TreeFamiTF321411.

    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 (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q8N8S7-1) [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

    MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG    50
    RKIQDHQVVI NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF 100
    ASAMMHALEV LNSQETGPTL PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ 150
    QRQKELERER LERERMERER LERERLERER LERERLEQEQ LERERQERER 200
    QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER ERQERERQEQ 250
    LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET 300
    PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP 350
    PPPPPLPNQV PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK 400
    LRKVSRMEDT SFPSGGNAIG VNSASSKTDT GRGNGPLPLG GSGLMEEMSA 450
    LLARRRRIAE KGSTIETEQK EDKGEDSEPV TSKASSTSTP EPTRKPWERT 500
    NTMNGSKSPV ISRRDSPRKN QIVFDNRSYD SLHRPKSTPL SQPSANGVQT 550
    EGLDYDRLKQ DILDEMRKEL TKLKEELIDA IRQELSKSNT A 591
    Length:591
    Mass (Da):66,510
    Last modified:June 7, 2004 - v2
    Checksum:iBF3252F6FCD1988B
    GO
    Isoform 2 (identifier: Q8N8S7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         514-534: Missing.

    Note: Contains a phosphothreonine at position 502. Contains a phosphoserine at position 512.

    Show »
    Length:570
    Mass (Da):63,924
    Checksum:i7BC390588F822497
    GO
    Isoform 3 (identifier: Q8N8S7-3) [UniParc]FASTAAdd to Basket

    Also known as: Deltav6

    The sequence of this isoform differs from the canonical sequence as follows:
         268-304: Missing.
         513-533: Missing.

    Note: Expression restricted to invasive cancer cells. Contains a phosphothreonine at position 465. Contains a phosphoserine at position 475.

    Show »
    Length:533
    Mass (Da):60,349
    Checksum:iF84762C64B6181C5
    GO

    Sequence cautioni

    The sequence BAA91799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAC04736.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAH71475.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22018.1 differs from that shown. Reason: Erroneous gene model prediction.
    The sequence CAI22020.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti493 – 4931T → I in AAH95481. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei268 – 30437Missing in isoform 3. 1 PublicationVSP_053772Add
    BLAST
    Alternative sequencei513 – 53321Missing in isoform 3. 1 PublicationVSP_053773Add
    BLAST
    Alternative sequencei514 – 53421Missing in isoform 2. 4 PublicationsVSP_010564Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY345143 mRNA. Translation: AAR04685.1.
    AF519769 mRNA. Translation: AAQ08487.1.
    EU255274 mRNA. Translation: ABY78022.1.
    AL591380, AC092811, AL356216 Genomic DNA. Translation: CAH71475.1. Sequence problems.
    AL591380, AC092811, AL356216 Genomic DNA. Translation: CAH71476.1.
    AL356216, AC092811 Genomic DNA. Translation: CAI22018.1. Sequence problems.
    AL356216, AL591380, AC092811 Genomic DNA. Translation: CAI22019.1.
    AL356216, AL591380, AC092811 Genomic DNA. Translation: CAI22020.1. Sequence problems.
    BC065238 mRNA. Translation: AAH65238.1.
    BC095481 mRNA. Translation: AAH95481.1.
    AK001635 mRNA. Translation: BAA91799.1. Different initiation.
    AK096246 mRNA. Translation: BAC04736.1. Different initiation.
    AL133059 mRNA. Translation: CAB61384.1.
    CCDSiCCDS31040.1. [Q8N8S7-2]
    CCDS31041.1. [Q8N8S7-1]
    PIRiT42661.
    RefSeqiNP_001008493.1. NM_001008493.1. [Q8N8S7-1]
    NP_060682.2. NM_018212.4. [Q8N8S7-2]
    UniGeneiHs.497893.

    Genome annotation databases

    EnsembliENST00000366843; ENSP00000355808; ENSG00000154380. [Q8N8S7-2]
    ENST00000366844; ENSP00000355809; ENSG00000154380. [Q8N8S7-1]
    GeneIDi55740.
    KEGGihsa:55740.
    UCSCiuc001hpc.1. human. [Q8N8S7-1]
    uc001hpd.1. human. [Q8N8S7-2]

    Polymorphism databases

    DMDMi48428086.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY345143 mRNA. Translation: AAR04685.1 .
    AF519769 mRNA. Translation: AAQ08487.1 .
    EU255274 mRNA. Translation: ABY78022.1 .
    AL591380 , AC092811 , AL356216 Genomic DNA. Translation: CAH71475.1 . Sequence problems.
    AL591380 , AC092811 , AL356216 Genomic DNA. Translation: CAH71476.1 .
    AL356216 , AC092811 Genomic DNA. Translation: CAI22018.1 . Sequence problems.
    AL356216 , AL591380 , AC092811 Genomic DNA. Translation: CAI22019.1 .
    AL356216 , AL591380 , AC092811 Genomic DNA. Translation: CAI22020.1 . Sequence problems.
    BC065238 mRNA. Translation: AAH65238.1 .
    BC095481 mRNA. Translation: AAH95481.1 .
    AK001635 mRNA. Translation: BAA91799.1 . Different initiation.
    AK096246 mRNA. Translation: BAC04736.1 . Different initiation.
    AL133059 mRNA. Translation: CAB61384.1 .
    CCDSi CCDS31040.1. [Q8N8S7-2 ]
    CCDS31041.1. [Q8N8S7-1 ]
    PIRi T42661.
    RefSeqi NP_001008493.1. NM_001008493.1. [Q8N8S7-1 ]
    NP_060682.2. NM_018212.4. [Q8N8S7-2 ]
    UniGenei Hs.497893.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2HO2 X-ray 1.33 B 347-356 [» ]
    2IYB X-ray 2.35 A/B/C/D 1-113 [» ]
    2XQN X-ray 2.62 M 1-116 [» ]
    ProteinModelPortali Q8N8S7.
    SMRi Q8N8S7. Positions 1-113.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 120858. 21 interactions.
    IntActi Q8N8S7. 12 interactions.
    MINTi MINT-3041121.
    STRINGi 9606.ENSP00000355809.

    PTM databases

    PhosphoSitei Q8N8S7.

    Polymorphism databases

    DMDMi 48428086.

    Proteomic databases

    MaxQBi Q8N8S7.
    PaxDbi Q8N8S7.
    PRIDEi Q8N8S7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366843 ; ENSP00000355808 ; ENSG00000154380 . [Q8N8S7-2 ]
    ENST00000366844 ; ENSP00000355809 ; ENSG00000154380 . [Q8N8S7-1 ]
    GeneIDi 55740.
    KEGGi hsa:55740.
    UCSCi uc001hpc.1. human. [Q8N8S7-1 ]
    uc001hpd.1. human. [Q8N8S7-2 ]

    Organism-specific databases

    CTDi 55740.
    GeneCardsi GC01M225674.
    HGNCi HGNC:18271. ENAH.
    HPAi HPA028448.
    HPA028696.
    MIMi 609061. gene.
    neXtProti NX_Q8N8S7.
    PharmGKBi PA38517.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289321.
    HOVERGENi HBG006655.
    KOi K05746.
    OrthoDBi EOG72JWGQ.
    PhylomeDBi Q8N8S7.
    TreeFami TF321411.

    Enzyme and pathway databases

    Reactomei REACT_12623. Generation of second messenger molecules.
    REACT_19351. Signaling by Robo receptor.

    Miscellaneous databases

    ChiTaRSi ENAH. human.
    EvolutionaryTracei Q8N8S7.
    GeneWikii ENAH_(gene).
    GenomeRNAii 55740.
    NextBioi 35488942.
    PROi Q8N8S7.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8N8S7.
    CleanExi HS_ENAH.
    Genevestigatori Q8N8S7.

    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. "Human Mena: cDNA cloning, expression and promoter characterization."
      Urbanelli L.
      Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    2. "Human Mena protein, a serex-defined antigen overexpressed in breast cancer eliciting both humoral and CD8+ T-cell immune response."
      Di Modugno F., Bronzi G., Scanlan M.J., Del Bello D., Cascioli S., Venturo I., Botti C., Nicotra M.R., Mottolese M., Natali P.G., Santoni A., Jager E., Nistico P.
      Int. J. Cancer 109:909-918(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Mammary tumor.
    3. "Splicing program of human MENA produces a previously undescribed isoform associated with invasive, mesenchymal-like breast tumors."
      Di Modugno F., Iapicca P., Boudreau A., Mottolese M., Terrenato I., Perracchio L., Carstens R.P., Santoni A., Bissell M.J., Nistico P.
      Proc. Natl. Acad. Sci. U.S.A. 109:19280-19285(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 44-591 (ISOFORM 2).
      Tissue: Placenta and Skin.
    6. "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] OF 85-591 (ISOFORM 2).
      Tissue: Teratocarcinoma.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-591 (ISOFORM 2).
      Tissue: Testis.
    8. "Cdc42 induces filopodia by promoting the formation of an IRSp53:Mena complex."
      Krugmann S., Jordens I., Gevaert K., Driessens M., Vandekerckhove J., Hall A.
      Curr. Biol. 11:1645-1655(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 23-47; 70-81; 123-145; 403-427; 484-499 AND 573-587, FUNCTION, INTERACTION WITH BAIAP2.
    9. "A novel proline-rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family."
      Niebuhr K., Ebel F., Frank R., Reinhard M., Domann E., Carl U.D., Walter U., Gertler F.B., Wehland J., Chakraborty T.
      EMBO J. 16:5433-5444(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VCL; ZYX AND L.MONOCYTOGENES ACTA.
    10. "Characterization of the interaction between zyxin and members of the Ena/vasodilator-stimulated phosphoprotein family of proteins."
      Drees B., Friederich E., Fradelizi J., Louvard D., Beckerle M.C., Golsteyn R.M.
      J. Biol. Chem. 275:22503-22511(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ZYX.
    11. "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.
    12. "RIAM, an Ena/VASP and profilin ligand, interacts with Rap1-GTP and mediates Rap1-induced adhesion."
      Lafuente E.M., van Puijenbroek A.A., Krause M., Carman C.V., Freeman G.J., Berezovskaya A., Constantine E., Springer T.A., Gertler F.B., Boussiotis V.A.
      Dev. Cell 7:585-595(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH APBB1IP.
      Tissue: T-cell.
    13. Cited for: SUBCELLULAR LOCATION.
    14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND SER-508, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-502 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-465 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND SER-508, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Structural basis for polyproline recognition by the FE65 WW domain."
      Meiyappan M., Birrane G., Ladias J.A.A.
      J. Mol. Biol. 372:970-980(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.33 ANGSTROMS) OF 347-356 IN COMPLEX WITH APBB1.
    20. "Tes, a specific Mena interacting partner, breaks the rules for EVH1 binding."
      Boeda B., Briggs D.C., Higgins T., Garvalov B.K., Fadden A.J., McDonald N.Q., Way M.
      Mol. Cell 28:1071-1082(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-113 IN COMPLEX WITH TES, INTERACTION WITH ZYX, FUNCTION, SUBCELLULAR LOCATION.
    21. "Molecular recognition of the Tes LIM2-3 domains by the actin-related protein Arp7A."
      Boeda B., Knowles P.P., Briggs D.C., Murray-Rust J., Soriano E., Garvalov B.K., McDonald N.Q., Way M.
      J. Biol. Chem. 286:11543-11554(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 1-116 IN COMPLEX WITH TES AND ACTL7A.

    Entry informationi

    Entry nameiENAH_HUMAN
    AccessioniPrimary (citable) accession number: Q8N8S7
    Secondary accession number(s): D0PQI2
    , Q502W5, Q5T5M7, Q5VTQ9, Q5VTR0, Q9NVF3, Q9UFB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 120 of the entry and version 2 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

    Miscellaneous

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

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

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

    External Data

    Dasty 3