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Q9UI08 (EVL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ena/VASP-like protein
Alternative name(s):
Ena/vasodilator-stimulated phosphoprotein-like
Gene names
Name:EVL
Synonyms:RNB6
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 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. EVL enhances actin nucleation and polymerization.

Subunit structure

Homotetramer By similarity. Binds to the SH3 domains of ABL1, LYN and SRC. Also binds to profilin, with preference for isoform IIaof PFN2, and the WW domain of APBB1/FE65. Binds to SEMA6A. Interacts, via the Pro-rich region, with the C-terminal SH3 domain of DNMBP. Interacts with RAPH1. Binds, via the EVH1 domain, the Pro-rich domain of Listeria monocytogenes actA By similarity. Binds, via the EVH1 domain, the Pro-rich domain of ZYX. Ref.9 Ref.10 Ref.11

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell projectionlamellipodium By similarity. Note: Targeted to the leading edge of lamellipodia and the dital tip of stress fibers through interaction with a number of proteins. In activated T-cells, localizes to the F-actin collar and the distal tip of microspikes By similarity.

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

Phosphorylated by PKA; phosphorylation abolishes binding to SH3 domains of ABL and SRC 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.

Ontologies

Keywords
   Cellular componentCell projection
Cytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainSH3-binding
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament organization

Traceable author statement PubMed 9268706. Source: ProtInc

actin polymerization or depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

axon guidance

Traceable author statement. Source: Reactome

cell surface receptor signaling pathway

Non-traceable author statement Ref.9. Source: UniProtKB

negative regulation of epithelial cell migration

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

negative regulation of ruffle assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

nervous system development

Non-traceable author statement Ref.9. Source: UniProtKB

organ morphogenesis

Non-traceable author statement Ref.9. Source: UniProtKB

positive regulation of stress fiber assembly

Inferred from mutant phenotype PubMed 23153535. Source: UniProt

protein homotetramerization

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

focal adhesion

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionSH3 domain binding

Inferred from sequence or structural similarity. Source: UniProtKB

profilin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 23275563PubMed 24705354. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 2 (identifier: Q9UI08-1)

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 1 (identifier: Q9UI08-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MAT

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Ena/VASP-like protein
PRO_0000087104

Regions

Domain1 – 112112WH1
Region222 – 413192EVH2
Region222 – 24221EVH2 block A
Region265 – 28218EVH2 block B
Region379 – 41335EVH2 block C
Motif231 – 2344KLKR
Compositional bias162 – 20645Pro-rich

Amino acid modifications

Modified residue2461Phosphoserine Ref.13
Modified residue3041Phosphoserine Ref.13 Ref.14
Modified residue3061Phosphoserine Ref.13
Modified residue3291Phosphoserine Ref.13
Modified residue3311Phosphoserine Ref.13
Modified residue3411Phosphoserine Ref.14
Modified residue3491Phosphoserine Ref.12 Ref.13
Modified residue3541Phosphoserine Ref.14
Modified residue3691Phosphoserine Ref.12

Natural variations

Alternative sequence11M → MAT in isoform 1.
VSP_004044
Natural variant1881P → L in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036464
Natural variant2471P → L in a colorectal cancer sample; somatic mutation. Ref.18
VAR_036465

Experimental info

Sequence conflict2011P → S in AAF17197. Ref.3
Sequence conflict3291S → N in AAP97156. Ref.2
Sequence conflict3641M → Y in CAB63763. Ref.8

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 [UniParc].

Last modified November 15, 2002. Version 2.
Checksum: AD5B67458755D659

FASTA41644,620
        10         20         30         40         50         60 
MSEQSICQAR ASVMVYDDTS KKWVPIKPGQ QGFSRINIYH NTASNTFRVV GVKLQDQQVV 

        70         80         90        100        110        120 
INYSIVKGLK YNQATPTFHQ WRDARQVYGL NFASKEEATT FSNAMLFALN IMNSQEGGPS 

       130        140        150        160        170        180 
SQRQVQNGPS PDEMDIQRRQ VMEQHQQQRQ ESLERRTSAT GPILPPGHPS SAASAPVSCS 

       190        200        210        220        230        240 
GPPPPPPPPV PPPPTGATPP PPPPLPAGGA QGSSHDESSM SGLAAAIAGA KLRRVQRPED 

       250        260        270        280        290        300 
ASGGSSPSGT SKSDANRASS GGGGGGLMEE MNKLLAKRRK AASQSDKPAE KKEDESQMED 

       310        320        330        340        350        360 
PSTSPSPGTR AASQPPNSSE AGRKPWERSN SVEKPVSSIL SRTPSVAKSP EAKSPLQSQP 

       370        380        390        400        410 
HSRMKPAGSV NDMALDAFDL DRMKQEILEE VVRELHKVKE EIIDAIRQEL SGISTT 

« Hide

Isoform 1 [UniParc].

Checksum: BFCCF68CF923720C
Show »

FASTA41844,792

References

« Hide 'large scale' references
[1]Ohta S., Mineta T., Kimoto M., Tabuchi K.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[2]"Cloning of a new human cDNA homologous to R.norvegicus RNB6 mRNA."
Wan Y.Z., Yu L., Yue P., Tu Q., Fu S.N., Zhao S.Y.
Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal gland.
[4]"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].
Tissue: Brain.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Lung and Pancreas.
[7]Mei G., Yu W., Gibbs R.A.
Submitted (FEB-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 55-416.
Tissue: Brain.
[8]"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 163-364.
Tissue: Uterus.
[9]"The orthologous human and murine semaphorin 6A-1 proteins (SEMA6A-1/Sema6A-1) bind to the enabled/vasodilator-stimulated phosphoprotein-like protein (EVL) via a novel carboxyl-terminal zyxin-like domain."
Klostermann A., Lutz B., Gertler F., Behl C.
J. Biol. Chem. 275:39647-39653(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SEMA6A.
[10]"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: INTERACTION WITH RAPH1.
[11]"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: INTERACTION WITH ZYX.
[12]"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment."
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.
J. Proteome Res. 7:5167-5176(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-349 AND SER-369, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: T-cell.
[13]"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-246; SER-304; SER-306; SER-329; SER-331 AND SER-349, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304; SER-341 AND SER-354, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-188 AND LEU-247.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF052504 mRNA. Translation: AAF21709.1.
AF087843 mRNA. Translation: AAP97156.1.
AF112209 mRNA. Translation: AAF17197.1.
AK289720 mRNA. Translation: BAF82409.1.
CH471061 Genomic DNA. Translation: EAW81684.1.
BC023997 mRNA. Translation: AAH23997.1.
BC032358 mRNA. Translation: AAH32358.1.
AF131766 mRNA. Translation: AAD20040.1.
AL133642 mRNA. Translation: CAB63763.2.
CCDSCCDS9955.1. [Q9UI08-2]
RefSeqNP_057421.1. NM_016337.2. [Q9UI08-2]
UniGeneHs.125867.

3D structure databases

ProteinModelPortalQ9UI08.
SMRQ9UI08. Positions 1-113.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119556. 17 interactions.
IntActQ9UI08. 8 interactions.
MINTMINT-3080348.
STRING9606.ENSP00000376652.

PTM databases

PhosphoSiteQ9UI08.

Polymorphism databases

DMDM25090276.

Proteomic databases

MaxQBQ9UI08.
PaxDbQ9UI08.
PRIDEQ9UI08.

Protocols and materials databases

DNASU51466.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392920; ENSP00000376652; ENSG00000196405. [Q9UI08-2]
ENST00000402714; ENSP00000384720; ENSG00000196405. [Q9UI08-1]
GeneID51466.
KEGGhsa:51466.
UCSCuc001ygt.3. human. [Q9UI08-1]
uc001ygu.3. human. [Q9UI08-2]

Organism-specific databases

CTD51466.
GeneCardsGC14P101159.
H-InvDBHIX0011964.
HGNCHGNC:20234. EVL.
HPAHPA018849.
neXtProtNX_Q9UI08.
PharmGKBPA134890866.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG265043.
HOVERGENHBG006655.
OMAQHRQESL.
OrthoDBEOG72JWGQ.
PhylomeDBQ9UI08.
TreeFamTF321411.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_6900. Immune System.
SignaLinkQ9UI08.

Gene expression databases

ArrayExpressQ9UI08.
BgeeQ9UI08.
CleanExHS_EVL.
GenevestigatorQ9UI08.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR011993. PH_like_dom.
IPR017354. Vasodilator_phosphoprotein.
IPR014885. VASP_tetra.
IPR000697. WH1/EVH1.
[Graphical view]
PfamPF08776. VASP_tetra. 1 hit.
PF00568. WH1. 1 hit.
[Graphical view]
PIRSFPIRSF038010. Vasodilator_Phospo. 1 hit.
SMARTSM00461. WH1. 1 hit.
[Graphical view]
PROSITEPS50229. WH1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEVL. human.
GeneWikiEnah/Vasp-like.
GenomeRNAi51466.
NextBio55097.
PROQ9UI08.

Entry information

Entry nameEVL_HUMAN
AccessionPrimary (citable) accession number: Q9UI08
Secondary accession number(s): A8K105 expand/collapse secondary AC list , O95884, Q7Z522, Q8TBV1, Q9UF25, Q9UIC2
Entry history
Integrated into UniProtKB/Swiss-Prot: November 15, 2002
Last sequence update: November 15, 2002
Last modified: July 9, 2014
This is version 130 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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM