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Q8N8S7

- ENAH_HUMAN

UniProt

Q8N8S7 - ENAH_HUMAN

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Protein
Protein enabled homolog
Gene
ENAH, MENA
Organism
Homo sapiens (Human)
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 By similarity.2 Publications

GO - Molecular functioni

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

GO - Biological processi

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

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
Complete GO annotation...

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 homolog
PRO_0000086971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei125 – 1251Phosphoserine3 Publications
Modified residuei265 – 2651Phosphoserine; by PKA By 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.6 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

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.

Miscellaneous databases

EvolutionaryTraceiQ8N8S7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 111111WH1
Add
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 – 588198EVH2
Add
BLAST
Regioni391 – 41121EVH2 block A
Add
BLAST
Regioni442 – 45918EVH2 block B
Add
BLAST
Regioni554 – 58835EVH2 block C
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili135 – 265131 Reviewed prediction
Add
BLAST
Coiled coili557 – 58731 Reviewed prediction
Add
BLAST

Motif

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi310 – 37364Pro-rich
Add
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.
Contains 1 WH1 domain.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei268 – 30437Missing in isoform 3.
VSP_053772Add
BLAST
Alternative sequencei513 – 53321Missing in isoform 3.
VSP_053773Add
BLAST
Alternative sequencei514 – 53421Missing in isoform 2.
VSP_010564Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti493 – 4931T → I in AAH95481. 1 Publication

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

« 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. "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: September 3, 2014
This is version 119 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

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