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Q8N8S7 (ENAH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein enabled homolog
Gene names
Name:ENAH
Synonyms:MENA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length591 AA.
Sequence statusComplete.
Protein existenceEvidence 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.8 Ref.20

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.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.20

Subcellular location

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. Ref.13 Ref.20

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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FAT1Q145172EBI-2834410,EBI-1171918

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: Q8N8S7-3)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 591591Protein enabled homolog
PRO_0000086971

Regions

Domain1 – 111111WH1
Repeat156 – 16051
Repeat161 – 16552
Repeat166 – 17053
Repeat171 – 17554
Repeat176 – 18055
Repeat181 – 18556
Repeat186 – 19057
Repeat191 – 19558
Repeat196 – 20059
Region156 – 200459 X 5 AA tandem repeats of [LMQ]-E-[QR]-E-[QR]
Region391 – 588198EVH2
Region391 – 41121EVH2 block A
Region442 – 45918EVH2 block B
Region554 – 58835EVH2 block C
Coiled coil135 – 265131 Potential
Coiled coil557 – 58731 Potential
Motif400 – 4034KLKR
Compositional bias310 – 37364Pro-rich

Amino acid modifications

Modified residue1251Phosphoserine Ref.14 Ref.15 Ref.16
Modified residue2651Phosphoserine; by PKA By similarity
Modified residue5061Phosphoserine Ref.15 Ref.16
Modified residue5081Phosphoserine Ref.15 Ref.16

Natural variations

Alternative sequence268 – 30437Missing in isoform 3.
VSP_053772
Alternative sequence513 – 53321Missing in isoform 3.
VSP_053773
Alternative sequence514 – 53421Missing in isoform 2.
VSP_010564

Experimental info

Sequence conflict4931T → I in AAH95481. Ref.5

Secondary structure

.................. 591
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 7, 2004. Version 2.
Checksum: BF3252F6FCD1988B

FASTA59166,510
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 7BC390588F822497
Show »

FASTA57063,924
Isoform 3 (Deltav6) [UniParc].

Checksum: F84762C64B6181C5
Show »

FASTA53360,349

References

« Hide '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]"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. expand/collapse author list , 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. expand/collapse author list , 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]"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.
[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]"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.
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[15]"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), 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]"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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRT42661.
RefSeqNP_001008493.1. NM_001008493.1.
NP_060682.2. NM_018212.4.
UniGeneHs.497893.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HO2X-ray1.33B347-356[»]
2IYBX-ray2.35A/B/C/D1-113[»]
2XQNX-ray2.62M1-116[»]
ProteinModelPortalQ8N8S7.
SMRQ8N8S7. Positions 1-113, 549-588.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120858. 19 interactions.
IntActQ8N8S7. 12 interactions.
MINTMINT-3041121.
STRING9606.ENSP00000355809.

PTM databases

PhosphoSiteQ8N8S7.

Polymorphism databases

DMDM48428086.

Proteomic databases

PaxDbQ8N8S7.
PRIDEQ8N8S7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366843; ENSP00000355808; ENSG00000154380. [Q8N8S7-2]
ENST00000366844; ENSP00000355809; ENSG00000154380. [Q8N8S7-1]
GeneID55740.
KEGGhsa:55740.
UCSCuc001hpc.1. human. [Q8N8S7-1]
uc001hpd.1. human. [Q8N8S7-2]

Organism-specific databases

CTD55740.
GeneCardsGC01M225674.
HGNCHGNC:18271. ENAH.
HPAHPA028448.
HPA028696.
MIM609061. gene.
neXtProtNX_Q8N8S7.
PharmGKBPA38517.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289321.
HOVERGENHBG006655.
KOK05746.
OrthoDBEOG72JWGQ.
PhylomeDBQ8N8S7.
TreeFamTF321411.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.

Gene expression databases

BgeeQ8N8S7.
CleanExHS_ENAH.
GenevestigatorQ8N8S7.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR000156. Ran_bind_dom.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
SMARTSM00160. RanBD. 1 hit.
SM00461. WH1. 1 hit.
[Graphical view]
PROSITEPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSENAH. human.
EvolutionaryTraceQ8N8S7.
GeneWikiENAH_(gene).
GenomeRNAi55740.
NextBio60693.
PROQ8N8S7.
SOURCESearch...

Entry information

Entry nameENAH_HUMAN
AccessionPrimary (citable) accession number: Q8N8S7
Secondary accession number(s): D0PQI2 expand/collapse secondary AC list , Q502W5, Q5T5M7, Q5VTQ9, Q5VTR0, Q9NVF3, Q9UFB8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 19, 2014
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM