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Q03173

- ENAH_MOUSE

UniProt

Q03173 - ENAH_MOUSE

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Protein

Protein enabled homolog

Gene

Enah

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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. 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
Complete GO annotation...

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-KW
Complete GO annotation...

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

BgeeiQ03173.
CleanExiMM_ENAH.
ExpressionAtlasiQ03173. baseline and differential.
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

        10         20         30         40         50
MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG
60 70 80 90 100
RKIQDHQVVI NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF
110 120 130 140 150
ASAMMHALEV LNSQEAAQSK VTATQDSTNL RCIFCGPTLP RQNSQLPAQV
160 170 180 190 200
QNGPSQEELE IQRRQLQEQQ RQKELERERM ERERLERERL ERERLERERL
210 220 230 240 250
EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ LEREQVEWER
260 270 280 290 300
ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD
310 320 330 340 350
YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN
360 370 380 390 400
SRPSSPVNTP SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP
410 420 430 440 450
VLPVCVSSPV PQMPPSPTAP NGSLDSVTYP VSPPPTSGPA APPPPPPPPP
460 470 480 490 500
PPPPPPLPPP PLPPLASLSH CGSQASPPPG TPLASTPSSK PSVLPSPSAG
510 520 530 540 550
APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL GPPAPPPPPP
560 570 580 590 600
LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP
610 620 630 640 650
APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT
660 670 680 690 700
GSVSLASSKA DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE
710 720 730 740 750
QKEDRNEDAE PITAKAPSTS TPEPTRKPWE RTNTMNGSKS PVISRPKSTP
760 770 780 790 800
SSQPSANGVQ TEGLDYDRLK QDILDEMRKE LAKLKEELID AIRQELSKSN

TA
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

Bgeei Q03173.
CleanExi MM_ENAH.
ExpressionAtlasi Q03173. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 132 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