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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 similarity2 Publications

GO - Molecular functioni

  • WW domain binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding

Enzyme and pathway databases

ReactomeiR-HSA-202433. Generation of second messenger molecules.
R-HSA-376176. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:18271. ENAH.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Synapse

Pathology & Biotechi

Organism-specific databases

DisGeNETi55740.
OpenTargetsiENSG00000154380.
PharmGKBiPA38517.

Polymorphism and mutation databases

BioMutaiENAH.
DMDMi48428086.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000869711 – 591Protein enabled homologAdd BLAST591

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei125PhosphoserineCombined sources1
Modified residuei265Phosphoserine; by PKABy similarity1
Modified residuei506PhosphoserineCombined sources1
Modified residuei508PhosphoserineCombined sources1
Isoform 3 (identifier: Q8N8S7-3)
Modified residuei465PhosphothreonineCombined sources1
Modified residuei471PhosphoserineCombined sources1
Modified residuei475PhosphoserineCombined sources1
Isoform 2 (identifier: Q8N8S7-2)
Modified residuei502PhosphothreonineCombined sources1
Modified residuei508PhosphoserineCombined sources1
Modified residuei512PhosphoserineCombined sources1

Post-translational modificationi

NTN1-induced PKA phosphorylation on Ser-265 directly parallels the formation of filopodial protrusions.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N8S7.
MaxQBiQ8N8S7.
PaxDbiQ8N8S7.
PeptideAtlasiQ8N8S7.
PRIDEiQ8N8S7.

PTM databases

iPTMnetiQ8N8S7.
PhosphoSitePlusiQ8N8S7.

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

BgeeiENSG00000154380.
CleanExiHS_ENAH.
ExpressionAtlasiQ8N8S7. baseline and differential.
GenevisibleiQ8N8S7. HS.

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
TERF2IPQ9NYB02EBI-2834410,EBI-750109
TESQ9UGI82EBI-2834410,EBI-2561654

GO - Molecular functioni

  • WW domain binding Source: UniProtKB

Protein-protein interaction databases

BioGridi120858. 40 interactors.
IntActiQ8N8S7. 21 interactors.
MINTiMINT-3041121.
STRINGi9606.ENSP00000355809.

Structurei

Secondary structure

1591
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 17Combined sources15
Turni18 – 21Combined sources4
Beta strandi22 – 25Combined sources4
Helixi26 – 28Combined sources3
Beta strandi32 – 40Combined sources9
Turni41 – 44Combined sources4
Beta strandi45 – 52Combined sources8
Turni53 – 55Combined sources3
Beta strandi58 – 64Combined sources7
Beta strandi74 – 81Combined sources8
Beta strandi86 – 93Combined sources8
Helixi94 – 110Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8N8S7.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 111WH1PROSITE-ProRule annotationAdd BLAST111
Repeati156 – 16015
Repeati161 – 16525
Repeati166 – 17035
Repeati171 – 17545
Repeati176 – 18055
Repeati181 – 18565
Repeati186 – 19075
Repeati191 – 19585
Repeati196 – 20095

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni156 – 2009 X 5 AA tandem repeats of [LMQ]-E-[QR]-E-[QR]Add BLAST45
Regioni391 – 588EVH2Add BLAST198
Regioni391 – 411EVH2 block AAdd BLAST21
Regioni442 – 459EVH2 block BAdd BLAST18
Regioni554 – 588EVH2 block CAdd BLAST35

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili135 – 265Sequence analysisAdd BLAST131
Coiled coili557 – 587Sequence analysisAdd BLAST31

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi400 – 403KLKR4

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi310 – 373Pro-richAdd BLAST64

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

eggNOGiKOG4590. Eukaryota.
ENOG41101TS. LUCA.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiQ8N8S7.
KOiK05746.
OMAiGFFSGSM.
OrthoDBiEOG091G0QTE.
PhylomeDBiQ8N8S7.
TreeFamiTF321411.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
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.

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.Combined sources
Show »
Length:533
Mass (Da):60,349
Checksum:iF84762C64B6181C5
GO

Sequence cautioni

The sequence BAA91799 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC04736 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence CAH71475 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI22018 differs from that shown. Reason: Erroneous gene model prediction.Curated
The sequence CAI22020 differs from that shown. Reason: Erroneous gene model prediction.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti493T → I in AAH95481 (PubMed:15489334).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_053772268 – 304Missing in isoform 3. 1 PublicationAdd BLAST37
Alternative sequenceiVSP_053773513 – 533Missing in isoform 3. 1 PublicationAdd BLAST21
Alternative sequenceiVSP_010564514 – 534Missing in isoform 2. 4 PublicationsAdd BLAST21

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_001008493.2. [Q8N8S7-1]
NP_060682.2. NM_018212.5. [Q8N8S7-2]
UniGeneiHs.497893.

Genome annotation databases

EnsembliENST00000366843; ENSP00000355808; ENSG00000154380. [Q8N8S7-2]
ENST00000366844; ENSP00000355809; ENSG00000154380. [Q8N8S7-1]
GeneIDi55740.
KEGGihsa:55740.
UCSCiuc001hpc.2. human. [Q8N8S7-1]

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_001008493.2. [Q8N8S7-1]
NP_060682.2. NM_018212.5. [Q8N8S7-2]
UniGeneiHs.497893.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120858. 40 interactors.
IntActiQ8N8S7. 21 interactors.
MINTiMINT-3041121.
STRINGi9606.ENSP00000355809.

PTM databases

iPTMnetiQ8N8S7.
PhosphoSitePlusiQ8N8S7.

Polymorphism and mutation databases

BioMutaiENAH.
DMDMi48428086.

Proteomic databases

EPDiQ8N8S7.
MaxQBiQ8N8S7.
PaxDbiQ8N8S7.
PeptideAtlasiQ8N8S7.
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.2. human. [Q8N8S7-1]

Organism-specific databases

CTDi55740.
DisGeNETi55740.
GeneCardsiENAH.
HGNCiHGNC:18271. ENAH.
HPAiHPA028448.
HPA028696.
MIMi609061. gene.
neXtProtiNX_Q8N8S7.
OpenTargetsiENSG00000154380.
PharmGKBiPA38517.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4590. Eukaryota.
ENOG41101TS. LUCA.
GeneTreeiENSGT00730000110272.
HOVERGENiHBG006655.
InParanoidiQ8N8S7.
KOiK05746.
OMAiGFFSGSM.
OrthoDBiEOG091G0QTE.
PhylomeDBiQ8N8S7.
TreeFamiTF321411.

Enzyme and pathway databases

ReactomeiR-HSA-202433. Generation of second messenger molecules.
R-HSA-376176. Signaling by Robo receptor.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000154380.
CleanExiHS_ENAH.
ExpressionAtlasiQ8N8S7. baseline and differential.
GenevisibleiQ8N8S7. HS.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR011993. PH_dom-like.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1_dom.
[Graphical view]
PfamiPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
SMARTiSM00461. WH1. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 144 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

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 one 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.