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Protein

Protein enabled homolog

Gene

ENAH

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 (By similarity).By similarity

GO - Molecular functioni

  • WW domain binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18271. ENAH.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • filopodium Source: UniProtKB-SubCell
  • focal adhesion Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • plasma membrane Source: HPA
  • stress fiber Source: Ensembl
  • synapse Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38517.

Polymorphism and mutation databases

BioMutaiENAH.
DMDMi48428086.

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.
ExpressionAtlasiQ8N8S7. baseline and differential.
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. 29 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 strandi3 – 1715Combined sources
Turni18 – 214Combined sources
Beta strandi22 – 254Combined sources
Helixi26 – 283Combined sources
Beta strandi32 – 409Combined sources
Turni41 – 444Combined sources
Beta strandi45 – 528Combined sources
Turni53 – 553Combined sources
Beta strandi58 – 647Combined sources
Beta strandi74 – 818Combined sources
Beta strandi86 – 938Combined sources
Helixi94 – 11017Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HO2X-ray1.33B347-356[»]
2IYBX-ray2.35A/B/C/D1-113[»]
2XQNX-ray2.62M1-116[»]
4MY6X-ray1.70A/B1-111[»]
ProteinModelPortaliQ8N8S7.
SMRiQ8N8S7. Positions 1-111.
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.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiQ8N8S7.
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_dom.
[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. AlignAdd to basket

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

        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 LNSQETGPTL PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ
160 170 180 190 200
QRQKELERER LERERMERER LERERLERER LERERLEQEQ LERERQERER
210 220 230 240 250
QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER ERQERERQEQ
260 270 280 290 300
LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET
310 320 330 340 350
PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP
360 370 380 390 400
PPPPPLPNQV PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK
410 420 430 440 450
LRKVSRMEDT SFPSGGNAIG VNSASSKTDT GRGNGPLPLG GSGLMEEMSA
460 470 480 490 500
LLARRRRIAE KGSTIETEQK EDKGEDSEPV TSKASSTSTP EPTRKPWERT
510 520 530 540 550
NTMNGSKSPV ISRRDSPRKN QIVFDNRSYD SLHRPKSTPL SQPSANGVQT
560 570 580 590
EGLDYDRLKQ DILDEMRKEL TKLKEELIDA IRQELSKSNT A
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. Contains a phosphoserine at position 508.3 Publications

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. Contains a phosphoserine at position 471.3 Publications

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

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:
EMBLi
GenBanki
DDBJi
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]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HO2X-ray1.33B347-356[»]
2IYBX-ray2.35A/B/C/D1-113[»]
2XQNX-ray2.62M1-116[»]
4MY6X-ray1.70A/B1-111[»]
ProteinModelPortaliQ8N8S7.
SMRiQ8N8S7. Positions 1-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120858. 29 interactions.
IntActiQ8N8S7. 12 interactions.
MINTiMINT-3041121.
STRINGi9606.ENSP00000355809.

PTM databases

PhosphoSiteiQ8N8S7.

Polymorphism and mutation databases

BioMutaiENAH.
DMDMi48428086.

Proteomic databases

MaxQBiQ8N8S7.
PaxDbiQ8N8S7.
PRIDEiQ8N8S7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]

Organism-specific databases

CTDi55740.
GeneCardsiGC01M225674.
HGNCiHGNC:18271. ENAH.
HPAiHPA028448.
HPA028696.
MIMi609061. gene.
neXtProtiNX_Q8N8S7.
PharmGKBiPA38517.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289321.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiQ8N8S7.
KOiK05746.
OrthoDBiEOG72JWGQ.
PhylomeDBiQ8N8S7.
TreeFamiTF321411.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiENAH. human.
EvolutionaryTraceiQ8N8S7.
GeneWikiiENAH_(gene).
GenomeRNAii55740.
NextBioi35488942.
PROiQ8N8S7.
SOURCEiSearch...

Gene expression databases

BgeeiQ8N8S7.
CleanExiHS_ENAH.
ExpressionAtlasiQ8N8S7. baseline and differential.
GenevestigatoriQ8N8S7.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-508 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-471 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  20. "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.
  21. "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.
  22. "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: May 27, 2015
This is version 128 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.