Protein enabled homolog - Mus musculus (Mouse)

Preferred order of sections

Names and origin

Protein names

Recommended name:
Protein enabled homolog

Alternative name(s):
NPC-derived proline-rich protein 1
Short name=NDPP-1

Gene names

Name:	Enah
Synonyms:	Mena, Ndpp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	802 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.2 Ref.5 Ref.6 Ref.12
Subunit structure	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). Ref.2 Ref.4 Ref.7 Ref.8 Ref.9 Ref.10 Ref.13
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton By similarity. Cell projection › lamellipodium By similarity. Cell projection › filopodium By similarity. Cell junction › synapse By similarity. Cell junction › focal 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. Ref.2 Ref.5 Ref.6
Tissue specificity	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. Ref.1 Ref.2 Ref.5
Developmental stage	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). Ref.5
Domain	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.
Post-translational modification	NTN1-induced PKA phosphorylation on Ser-255 directly parallels the formation of filopodial protrusions.
Disruption phenotype	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. Ref.5
Miscellaneous	Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes.
Sequence similarities	Belongs to the Ena/VASP family. Contains 1 WH1 domain.
Sequence caution	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.

Ontologies

Keywords
Biological process	Differentiation Neurogenesis
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Synapse
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat SH3-binding
Ligand	Actin-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin polymerization or depolymerization Inferred from direct assay Ref.2. Source: MGI axon guidance Inferred from mutant phenotype Ref.5 PubMed 15371503. Source: MGI cellular component movement Inferred from direct assay Ref.2. Source: UniProtKB intracellular transport Inferred from electronic annotation. Source: InterPro neural tube closure Inferred from genetic interaction Ref.5 PubMed 15371503. Source: MGI
Cellular_component	cytosol Traceable author statement. Source: Reactome filopodium Inferred from direct assay Ref.5 Ref.10. Source: MGI focal adhesion Inferred from direct assay Ref.2. Source: UniProtKB lamellipodium Inferred from direct assay Ref.8 Ref.10. Source: MGI stress fiber Inferred from direct assay Ref.2. Source: MGI synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	SH3 domain binding Inferred from direct assay PubMed 9126384. Source: MGI profilin binding Inferred from direct assay Ref.5. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAIAP2	Q9UQB8	3	EBI-6083294,EBI-525456	From a different organism.

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 5 (identifier: Q03173-1) 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.

Isoform 1 (identifier: Q03173-2) The sequence of this isoform differs from the canonical sequence as follows: 1-412: Missing.
Note: No experimental confirmation available.

Isoform 2 (identifier: Q03173-3) 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.

Isoform 3 (identifier: Q03173-4) 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.

Isoform 4 (identifier: Q03173-5) 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

Isoform 6 (identifier: Q03173-6) 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

Protein enabled homolog

PRO_0000086972

Regions

Domain

1 – 111

111

WH1

Repeat

175 – 179

5

1

Repeat

180 – 184

5

2

Repeat

185 – 189

5

3

Repeat

190 – 194

5

4

Repeat

195 – 199

5

Repeat

200 – 204

5

6

Repeat

205 – 209

5

7

Region

175 – 209

35

7 X 5 AA tandem repeats of [LM]-E-[QR]-[EQ]-[QR]

Region

623 – 799

177

EVH2

Region

623 – 643

21

EVH2 block A

Region

674 – 691

18

EVH2 block B

Region

765 – 799

35

EVH2 block C

Coiled coil

154 – 258

105

Potential

Coiled coil

767 – 797

31

Potential

Motif

632 – 635

4

KLKR

Compositional bias

269 – 605

337

Pro-rich

Amino acid modifications

Modified residue

144

1

Phosphoserine Ref.11

Modified residue

255

1

Phosphoserine; by PKA Ref.12

Modified residue

557

1

Phosphotyrosine Ref.8

Modified residue

738

1

Phosphoserine By similarity

Modified residue

740

1

Phosphoserine By similarity

Natural variations

Alternative sequence

1 – 412

412

Missing in isoform 1.

VSP_007255

Alternative sequence

117 – 135

19

Missing in isoform 2, isoform 3 and isoform 6.

VSP_007259

Alternative sequence

117 – 131

15

Missing in isoform 4.

VSP_007257

Alternative sequence

132 – 135

4

CIFC → VFYL in isoform 4.

VSP_007258

Alternative sequence

259 – 500

242

Missing in isoform 2 and isoform 6.

VSP_007260

Alternative sequence

561 – 594

34

Missing in isoform 6.

VSP_010565

Experimental info

Mutagenesis

255

1

S → 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. Ref.6

Mutagenesis

255

1

S → 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. Ref.6

Mutagenesis

637

1

S → 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. Ref.6

Mutagenesis

637

1

S → 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. Ref.6

Sequence conflict

500

1

G → A in BAA01570. Ref.1

Secondary structure

1

.

802

Helix Strand Turn

Details...

Sequences

Sequence		Length	Mass (Da)
Isoform 5 (Neural variant Mena+++) (140 kDa isoform) [UniParc]. Last modified April 23, 2003. Version 2. Checksum: 592BB975EE20F77F Show »	FASTA	802	85,844
10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAAQSK 130 140 150 160 170 180 VTATQDSTNL RCIFCGPTLP RQNSQLPAQV QNGPSQEELE IQRRQLQEQQ RQKELERERM 190 200 210 220 230 240 ERERLERERL ERERLERERL EQEQLERQRQ EREHVERLER ERLERLERER QERERERLEQ 250 260 270 280 290 300 LEREQVEWER ERRMSNAAPS SDSSLSSAPL PEYSSCQPPS APPPSYAKVI SAPVSDATPD 310 320 330 340 350 360 YAVVTALPPT STPPTPPLRH AATRFATSLG SAFHPVLPHY ATVPRPLNKN SRPSSPVNTP 370 380 390 400 410 420 SSQPPAAKSC AWPTSNFSPL PPSPPIMISS PPGKATGPRP VLPVCVSSPV PQMPPSPTAP 430 440 450 460 470 480 NGSLDSVTYP VSPPPTSGPA APPPPPPPPP PPPPPPLPPP PLPPLASLSH CGSQASPPPG 490 500 510 520 530 540 TPLASTPSSK PSVLPSPSAG APASAETPLN PELGDSSASE PGLQAASQPA ESPTPQGLVL 550 560 570 580 590 600 GPPAPPPPPP LPSGPAYASA LPPPPGPPPP PPLPSTGPPP PPPPPPPLPN QAPPPPPPPP 610 620 630 640 650 660 APPLPASGIF SGSTSEDNRP LTGLAAAIAG AKLRKVSRVE DGSFPGGGNT GSVSLASSKA 670 680 690 700 710 720 DAGRGNGPLP LGGSGLMEEM SALLARRRRI AEKGSTIETE QKEDRNEDAE PITAKAPSTS 730 740 750 760 770 780 TPEPTRKPWE RTNTMNGSKS PVISRPKSTP SSQPSANGVQ TEGLDYDRLK QDILDEMRKE 790 800 LAKLKEELID AIRQELSKSN TA « Hide
Isoform 1 [UniParc]. Checksum: 1AA5DDB306450847 Show »	FASTA	390	39,306
10 20 30 40 50 60 MPPSPTAPNG SLDSVTYPVS PPPTSGPAAP PPPPPPPPPP PPPPLPPPPL PPLASLSHCG 70 80 90 100 110 120 SQASPPPGTP LASTPSSKPS VLPSPSAGAP ASAETPLNPE LGDSSASEPG LQAASQPAES 130 140 150 160 170 180 PTPQGLVLGP PAPPPPPPLP SGPAYASALP PPPGPPPPPP LPSTGPPPPP PPPPPLPNQA 190 200 210 220 230 240 PPPPPPPPAP PLPASGIFSG STSEDNRPLT GLAAAIAGAK LRKVSRVEDG SFPGGGNTGS 250 260 270 280 290 300 VSLASSKADA GRGNGPLPLG GSGLMEEMSA LLARRRRIAE KGSTIETEQK EDRNEDAEPI 310 320 330 340 350 360 TAKAPSTSTP EPTRKPWERT NTMNGSKSPV ISRPKSTPSS QPSANGVQTE GLDYDRLKQD 370 380 390 ILDEMRKELA KLKEELIDAI RQELSKSNTA « Hide
Isoform 2 (Mena) (80 kDa isoform) [UniParc]. Checksum: 19B25FD175DF0451 Show »	FASTA	541	59,643
10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAGPTL 130 140 150 160 170 180 PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER MERERLERER LERERLERER 190 200 210 220 230 240 LEQEQLERQR QEREHVERLE RERLERLERE RQERERERLE QLEREQVEWE RERRMSNAAA 250 260 270 280 290 300 PASAETPLNP ELGDSSASEP GLQAASQPAE SPTPQGLVLG PPAPPPPPPL PSGPAYASAL 310 320 330 340 350 360 PPPPGPPPPP PLPSTGPPPP PPPPPPLPNQ APPPPPPPPA PPLPASGIFS GSTSEDNRPL 370 380 390 400 410 420 TGLAAAIAGA KLRKVSRVED GSFPGGGNTG SVSLASSKAD AGRGNGPLPL GGSGLMEEMS 430 440 450 460 470 480 ALLARRRRIA EKGSTIETEQ KEDRNEDAEP ITAKAPSTST PEPTRKPWER TNTMNGSKSP 490 500 510 520 530 540 VISRPKSTPS SQPSANGVQT EGLDYDRLKQ DILDEMRKEL AKLKEELIDA IRQELSKSNT A « Hide
Isoform 3 (Neural variant Mena+) [UniParc]. Checksum: 5E610BE7FDDA97FE Show »	FASTA	783	83,776
10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAGPTL 130 140 150 160 170 180 PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER MERERLERER LERERLERER 190 200 210 220 230 240 LEQEQLERQR QEREHVERLE RERLERLERE RQERERERLE QLEREQVEWE RERRMSNAAP 250 260 270 280 290 300 SSDSSLSSAP LPEYSSCQPP SAPPPSYAKV ISAPVSDATP DYAVVTALPP TSTPPTPPLR 310 320 330 340 350 360 HAATRFATSL GSAFHPVLPH YATVPRPLNK NSRPSSPVNT PSSQPPAAKS CAWPTSNFSP 370 380 390 400 410 420 LPPSPPIMIS SPPGKATGPR PVLPVCVSSP VPQMPPSPTA PNGSLDSVTY PVSPPPTSGP 430 440 450 460 470 480 AAPPPPPPPP PPPPPPPLPP PPLPPLASLS HCGSQASPPP GTPLASTPSS KPSVLPSPSA 490 500 510 520 530 540 GAPASAETPL NPELGDSSAS EPGLQAASQP AESPTPQGLV LGPPAPPPPP PLPSGPAYAS 550 560 570 580 590 600 ALPPPPGPPP PPPLPSTGPP PPPPPPPPLP NQAPPPPPPP PAPPLPASGI FSGSTSEDNR 610 620 630 640 650 660 PLTGLAAAIA GAKLRKVSRV EDGSFPGGGN TGSVSLASSK ADAGRGNGPL PLGGSGLMEE 670 680 690 700 710 720 MSALLARRRR IAEKGSTIET EQKEDRNEDA EPITAKAPST STPEPTRKPW ERTNTMNGSK 730 740 750 760 770 780 SPVISRPKST PSSQPSANGV QTEGLDYDRL KQDILDEMRK ELAKLKEELI DAIRQELSKS NTA « Hide
Isoform 4 (Neural variant Mena++) [UniParc]. Checksum: 18C228F070EDCCF2 Show »	FASTA	787	84,299
10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAVFYL 130 140 150 160 170 180 GPTLPRQNSQ LPAQVQNGPS QEELEIQRRQ LQEQQRQKEL ERERMERERL ERERLERERL 190 200 210 220 230 240 ERERLEQEQL ERQRQEREHV ERLERERLER LERERQERER ERLEQLEREQ VEWERERRMS 250 260 270 280 290 300 NAAPSSDSSL SSAPLPEYSS CQPPSAPPPS YAKVISAPVS DATPDYAVVT ALPPTSTPPT 310 320 330 340 350 360 PPLRHAATRF ATSLGSAFHP VLPHYATVPR PLNKNSRPSS PVNTPSSQPP AAKSCAWPTS 370 380 390 400 410 420 NFSPLPPSPP IMISSPPGKA TGPRPVLPVC VSSPVPQMPP SPTAPNGSLD SVTYPVSPPP 430 440 450 460 470 480 TSGPAAPPPP PPPPPPPPPP PLPPPPLPPL ASLSHCGSQA SPPPGTPLAS TPSSKPSVLP 490 500 510 520 530 540 SPSAGAPASA ETPLNPELGD SSASEPGLQA ASQPAESPTP QGLVLGPPAP PPPPPLPSGP 550 560 570 580 590 600 AYASALPPPP GPPPPPPLPS TGPPPPPPPP PPLPNQAPPP PPPPPAPPLP ASGIFSGSTS 610 620 630 640 650 660 EDNRPLTGLA AAIAGAKLRK VSRVEDGSFP GGGNTGSVSL ASSKADAGRG NGPLPLGGSG 670 680 690 700 710 720 LMEEMSALLA RRRRIAEKGS TIETEQKEDR NEDAEPITAK APSTSTPEPT RKPWERTNTM 730 740 750 760 770 780 NGSKSPVISR PKSTPSSQPS ANGVQTEGLD YDRLKQDILD EMRKELAKLK EELIDAIRQE LSKSNTA « Hide
Isoform 6 (Mena(S)) [UniParc]. Checksum: FA0C43AAD240503C Show »	FASTA	507	56,357
10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQEAGPTL 130 140 150 160 170 180 PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER MERERLERER LERERLERER 190 200 210 220 230 240 LEQEQLERQR QEREHVERLE RERLERLERE RQERERERLE QLEREQVEWE RERRMSNAAA 250 260 270 280 290 300 PASAETPLNP ELGDSSASEP GLQAASQPAE SPTPQGLVLG PPAPPPPPPL PSGPAYASAP 310 320 330 340 350 360 PPPPPAPPLP ASGIFSGSTS EDNRPLTGLA AAIAGAKLRK VSRVEDGSFP GGGNTGSVSL 370 380 390 400 410 420 ASSKADAGRG NGPLPLGGSG LMEEMSALLA RRRRIAEKGS TIETEQKEDR NEDAEPITAK 430 440 450 460 470 480 APSTSTPEPT RKPWERTNTM NGSKSPVISR PKSTPSSQPS ANGVQTEGLD YDRLKQDILD 490 500 EMRKELAKLK EELIDAIRQE LSKSNTA « Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Mena is required for neurulation and commissure formation." Lanier L.M., Gates M.A., Witke W., Menzies A.S., Wehman A.M., Macklis J.D., Kwiatkowski D., Soriano P., Gertler F.B. Neuron 22:313-325(1999) [PubMed] [Europe PMC] [Abstract] 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]	"Phosphoproteomic analysis of the developing mouse brain." Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P. Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-144, MASS SPECTROMETRY. 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00284242.
IPI00284246.
IPI00417165.
IPI00468225.
IPI00470077.
IPI01008259.

PIR

S27200.

RefSeq

NP_001076589.1. NM_001083120.1.
NP_001076590.1. NM_001083121.1.
NP_032706.2. NM_008680.2.
NP_034265.2. NM_010135.2.

UniGene

Mm.389224.
Mm.87759.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EVH	X-ray	1.80	A	1-112	[»]

ProteinModelPortal

Q03173.

SMR

Q03173. Positions 1-113.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q03173. 2 interactions.

MINT

MINT-1215621.

PTM databases

PhosphoSite

Q03173.

Proteomic databases

PaxDb

Q03173.

PRIDE

Q03173.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000111025; ENSMUSP00000106654; ENSMUSG00000022995.

GeneID

13800.

KEGG

mmu:13800.

UCSC

uc007dxp.1. mouse.
uc007dxq.1. mouse.
uc007dxr.1. mouse.
uc007dxs.1. mouse.

Organism-specific databases

CTD

55740.

MGI

MGI:108360. Enah.

Phylogenomic databases

eggNOG

NOG289321.

GeneTree

ENSGT00440000039080.

HOGENOM

HOG000013015.

HOVERGEN

HBG006655.

InParanoid

Q03173.

KO

K05746.

OrthoDB

EOG437RF0.

Enzyme and pathway databases

Reactome

REACT_107772. Immune System.

Gene expression databases

ArrayExpress

Q03173.

Bgee

Q03173.

CleanEx

MM_ENAH.

Genevestigator

Q03173.

GermOnline

ENSMUSG00000022995. Mus musculus.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR000697. EVH1.
IPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR014885. VASP_tetra.
[Graphical view]

Pfam

PF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]

SMART

SM00160. RanBD. 1 hit.
SM00461. WH1. 1 hit.
[Graphical view]

PROSITE

PS50229. WH1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ENAH. mouse.

EvolutionaryTrace

Q03173.

NextBio

284558.

SOURCE

Search...

Entry information

Entry name

ENAH_MOUSE

Accession

Primary (citable) accession number: Q03173
Secondary accession number(s): P70430

Q5D053

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	April 23, 2003
Last modified:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Alternative products

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Natural variations

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents