Q8N8S7 (ENAH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Protein enabled homolog

Gene names

Name:	ENAH
Synonyms:	MENA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	591 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 By similarity. Ref.7 Ref.19
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 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. Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.19
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. 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.12 Ref.19
Tissue specificity	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. Ref.2
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-265 directly parallels the formation of filopodial protrusions By similarity.
Miscellaneous	Required to transform actin polymerization into active movement for the propulsive force of Listeria monocytogenes By similarity.
Sequence similarities	Belongs to the Ena/VASP family. Contains 1 WH1 domain.
Sequence caution	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.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Synapse
Coding sequence diversity	Alternative splicing
Domain	Coiled coil Repeat SH3-binding
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	T cell receptor signaling pathway Traceable author statement. Source: Reactome actin polymerization or depolymerization Inferred from electronic annotation. Source: Compara axon guidance Traceable author statement. Source: Reactome intracellular transport Inferred from electronic annotation. Source: InterPro neural tube closure Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome filopodium Inferred from electronic annotation. Source: UniProtKB-SubCell focal adhesion Inferred from direct assay. Source: HPA lamellipodium Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from direct assay. Source: HPA stress fiber Inferred from electronic annotation. Source: Compara synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q8N8S7-1)

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 2 (identifier: Q8N8S7-2)

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 591

591

Protein enabled homolog

PRO_0000086971

Regions

Domain

1 – 111

111

WH1

Repeat

156 – 160

5

1

Repeat

161 – 165

5

2

Repeat

166 – 170

5

3

Repeat

171 – 175

5

4

Repeat

176 – 180

5

5

Repeat

181 – 185

5

6

Repeat

186 – 190

5

7

Repeat

191 – 195

5

8

Repeat

196 – 200

5

9

Region

156 – 200

45

9 X 5 AA tandem repeats of [LMQ]-E-[QR]-E-[QR]

Region

391 – 588

198

EVH2

Region

391 – 411

21

EVH2 block A

Region

442 – 459

18

EVH2 block B

Region

554 – 588

35

EVH2 block C

Coiled coil

135 – 265

131

Potential

Coiled coil

557 – 587

31

Potential

Motif

400 – 403

4

KLKR

Compositional bias

310 – 373

64

Pro-rich

Amino acid modifications

Modified residue

125

1

Phosphoserine Ref.13 Ref.14 Ref.15

Modified residue

265

1

Phosphoserine; by PKA By similarity

Modified residue

506

1

Phosphoserine Ref.14 Ref.15

Modified residue

508

1

Phosphoserine Ref.14 Ref.15 Ref.17

Natural variations

Alternative sequence

514 – 534

21

Missing in isoform 2.

VSP_010564

Experimental info

Sequence conflict

493

1

T → I in AAH95481. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

591

Helix Strand Turn

Details...

Beta strand

4 – 17

14

Turn

18 – 21

4

Beta strand

22 – 25

4

Helix

26 – 28

3

Beta strand

33 – 40

8

Turn

41 – 44

4

Beta strand

45 – 52

8

Turn

53 – 55

3

Beta strand

58 – 63

6

Beta strand

74 – 81

8

Beta strand

86 – 93

8

Helix

94 – 111

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 7, 2004. Version 2. Checksum: BF3252F6FCD1988B	FASTA	591	66,510
	10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL 130 140 150 160 170 180 PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER LERERMERER LERERLERER 190 200 210 220 230 240 LERERLEQEQ LERERQERER QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER 250 260 270 280 290 300 ERQERERQEQ LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET 310 320 330 340 350 360 PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP PPPPPLPNQV 370 380 390 400 410 420 PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK LRKVSRMEDT SFPSGGNAIG 430 440 450 460 470 480 VNSASSKTDT GRGNGPLPLG GSGLMEEMSA LLARRRRIAE KGSTIETEQK EDKGEDSEPV 490 500 510 520 530 540 TSKASSTSTP EPTRKPWERT NTMNGSKSPV ISRRDSPRKN QIVFDNRSYD SLHRPKSTPL 550 560 570 580 590 SQPSANGVQT EGLDYDRLKQ DILDEMRKEL TKLKEELIDA IRQELSKSNT A
	Isoform 2 [UniParc]. Checksum: 7BC390588F822497	FASTA	570	63,924
	10 20 30 40 50 60 MSEQSICQAR AAVMVYDDAN KKWVPAGGST GFSRVHIYHH TGNNTFRVVG RKIQDHQVVI 70 80 90 100 110 120 NCAIPKGLKY NQATQTFHQW RDARQVYGLN FGSKEDANVF ASAMMHALEV LNSQETGPTL 130 140 150 160 170 180 PRQNSQLPAQ VQNGPSQEEL EIQRRQLQEQ QRQKELERER LERERMERER LERERLERER 190 200 210 220 230 240 LERERLEQEQ LERERQERER QERLERQERL ERQERLERQE RLDRERQERQ ERERLERLER 250 260 270 280 290 300 ERQERERQEQ LEREQLEWER ERRISSAAAP ASVETPLNSV LGDSSASEPG LQAASQPAET 310 320 330 340 350 360 PSQQGIVLGP LAPPPPPPLP PGPAQASVAL PPPPGPPPPP PLPSTGPPPP PPPPPLPNQV 370 380 390 400 410 420 PPPPPPPPAP PLPASGFFLA SMSEDNRPLT GLAAAIAGAK LRKVSRMEDT SFPSGGNAIG 430 440 450 460 470 480 VNSASSKTDT GRGNGPLPLG GSGLMEEMSA LLARRRRIAE KGSTIETEQK EDKGEDSEPV 490 500 510 520 530 540 TSKASSTSTP EPTRKPWERT NTMNGSKSPV ISRPKSTPLS QPSANGVQTE GLDYDRLKQD 550 560 570 ILDEMRKELT KLKEELIDAI RQELSKSNTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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].
[4]	"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.
[5]	"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.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 393-591 (ISOFORM 2). Tissue: Testis.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"Lamellipodin, an Ena/VASP ligand, is implicated in the regulation of lamellipodial dynamics." Krause M., Leslie J.D., Stewart M., Lafuente E.M., Valderrama F., Jagannathan R., Strasser G.A., Rubinson D.A., Liu H., Way M., Yaffe M.B., Boussiotis V.A., Gertler F.B. Dev. Cell 7:571-583(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[13]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-506 AND SER-508, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-502 (ISOFORM 2), MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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-508, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-512 (ISOFORM 2), MASS SPECTROMETRY.
[18]	"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.
[19]	"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.
[20]	"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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AY345143 mRNA. Translation: AAR04685.1.
AF519769 mRNA. Translation: AAQ08487.1.
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.

IPI

IPI00374054.
IPI00411623.

PIR

T42661.

RefSeq

NP_001008493.1. NM_001008493.1.
NP_060682.2. NM_018212.4.

UniGene

Hs.497893.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q8N8S7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8N8S7. 7 interactions.

MINT

MINT-3041121.

STRING

9606.ENSP00000355809.

PTM databases

PhosphoSite

Q8N8S7.

Polymorphism databases

DMDM

48428086.

Proteomic databases

PaxDb

Q8N8S7.

PRIDE

Q8N8S7.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000284563; ENSP00000284563; ENSG00000154380.
ENST00000366843; ENSP00000355808; ENSG00000154380.
ENST00000366844; ENSP00000355809; ENSG00000154380.

GeneID

55740.

KEGG

hsa:55740.

UCSC

uc001hpc.1. human.
uc001hpd.1. human.

Organism-specific databases

CTD

55740.

GeneCards

GC01M225674.

HGNC

HGNC:18271. ENAH.

HPA

HPA028448.
HPA028696.

MIM

609061. gene.

neXtProt

NX_Q8N8S7.

PharmGKB

PA38517.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG289321.

HOVERGEN

HBG006655.

KO

K05746.

OrthoDB

EOG437RF0.

PhylomeDB

Q8N8S7.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

Bgee

Q8N8S7.

CleanEx

HS_ENAH.

Genevestigator

Q8N8S7.

GermOnline

ENSG00000154380. Homo sapiens.

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. human.

EvolutionaryTrace

Q8N8S7.

GenomeRNAi

55740.

NextBio

60693.

SOURCE

Search...

Entry information

Entry name

ENAH_HUMAN

Accession

Primary (citable) accession number: Q8N8S7
Secondary accession number(s): Q502W5 , Q5T5M7, Q5VTQ9, Q5VTR0, Q9NVF3, Q9UFB8

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2004
Last sequence update:	June 7, 2004
Last modified:	May 1, 2013
This is version 107 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.